An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources
Abstract
:1. Introduction
2. Antimicrobial Peptides’ Natural Source
2.1. Viral AMPs
2.2. Bacterial AMPs
2.2.1. AMPs Made by Gram-Positive Bacteria
2.2.2. AMPs Made by Gram-Positive Bacteria
2.2.3. AMPs Made by Gram-Negative Bacteria
2.3. Fungal AMPs
2.4. Plant AMPs
2.4.1. Thionins
2.4.2. Hevein-like peptides
2.4.3. Defensins
2.4.4. Knottins
2.4.5. Stable-like Peptides
2.4.6. Snakins
2.4.7. Lipid Transfer Proteins
2.4.8. Cyclotides
2.5. Animal AMPs
3. Antimicrobial Peptide Structures and Activities
4. Antimicrobial Peptide Action
4.1. AMPs with Action on Cell Membranes
4.2. AMPs with No Action on Cell Membranes
5. AMP Potential in the Food Field
5.1. AMPs in Food Preservation
5.2. AMPs in Food Packaging
6. AMP Potential in the Pharmaceutical Field
6.1. AMP Antioxidant Potential
6.2. Antineoplastic Agent
6.3. AMP Potential against Respiratory Diseases
6.4. AMP Potential against Hypertension
6.5. AMP Potential against Obesity
6.6. AMP Potential against Intestine Infection and Inflammation
6.7. AMP Potential against Viral Infections
6.8. AMP Potential against Skin Infections
7. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Tang, S.S.; Prodhan, Z.H.; Biswas, S.K.; Le, C.F.; Sekaran, S.D. Antimicrobial peptides from different plant sources: Isolation, characterisation, and purification. Phytochemistry 2018, 154, 94–105. [Google Scholar] [CrossRef] [PubMed]
- Rai, M.; Pandit, R.; Gaikwad, S.; Kövics, G. Antimicrobial peptides as natural bio-preservative to enhance the shelf-life of food. J. Food Sci. Technol. 2016, 53, 3381–3394. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Johnstone, K.F.; Herzberg, M.C. Antimicrobial peptides: Defending the mucosal epithelial barrier. Front. Oral Health 2022, 3, 958480. [Google Scholar] [CrossRef] [PubMed]
- Liu, Y.; Sameen, D.E.; Ahmed, S.; Dai, J.; Qin, W. Antimicrobial peptides and their application in food packaging. Trends Food Sci. Technol. 2021, 112, 471–483. [Google Scholar] [CrossRef]
- Tam, J.P.; Wang, S.; Wong, K.H.; Tan, W.L. Antimicrobial Peptides from Plants. Pharmaceuticals 2015, 8, 711–757. [Google Scholar] [CrossRef]
- Dini, I. Chapter 14—Use of Essential Oils in Food Packaging. In Essential Oils in Food Preservation, Flavor and Safety; Academic Press: Cambridge, MA, USA, 2016; pp. 139–147. [Google Scholar]
- Upton, M.; Cotter, P.; Tagg, J. Antimicrobial peptides as therapeutic agents. Int. J. Microbiol. 2012, 2012, 326503. [Google Scholar] [CrossRef]
- Mahlapuu, M.; Håkansson, J.; Ringstad, L.; Björn, C. Antimicrobial peptides: An emerging category of therapeutic agents. Front. Cell. Infect. Microbiol. 2016, 6, 194. [Google Scholar] [CrossRef] [Green Version]
- Bin Hafeez, A.; Jiang, X.; Bergen, P.J.; Zhu, Y. Antimicrobial Peptides: An Update on Classifications and Databases. Int. J. Mol. Sci. 2021, 22, 11691. [Google Scholar] [CrossRef]
- Wang, C.K.; Craik, D.J. Designing macrocyclic disulfide-rich peptides for biotechnological applications perspective. Nat. Chem. Biol. 2018, 14, 417–427. [Google Scholar] [CrossRef]
- Henriques, S.T.; Lawrence, N.; Chaousis, S.; Ravipati, A.S.; Cheneval, O.; Benfield, A.H.; Elliott, A.G.; Kavanagh, A.M.; Cooper, M.A.; Chan, L.Y.; et al. Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties. ACS Chem. Biol. 2017, 12, 2324–2334. [Google Scholar] [CrossRef]
- Borah, A.; Deb, B.; Chakraborty, S. A Crosstalk on Antimicrobial Peptides. Int. J. Pept. Res. Ther. 2020, 27, 229–244. [Google Scholar] [CrossRef]
- Huan, Y.; Kong, Q.; Mou, H.; Yi, H. Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields. Front. Microbiol. 2020, 11, 582779. [Google Scholar] [CrossRef] [PubMed]
- Danis-Wlodarczyk, K.M.; Wozniak, D.J.; Abedon, S.T. Treating Bacterial Infections with Bacteriophage-Based Enzybiotics: In Vitro, In Vivo and Clinical Application. Antibiotics 2021, 10, 1497. [Google Scholar] [CrossRef] [PubMed]
- Nelson, D.; Loomis, L.; Fischetti, V.A. Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme. Proc. Natl. Acad. Sci. USA 2001, 98, 4107–4112. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Abdelrahman, F.; Easwaran, M.; Daramola, O.I.; Ragab, S.; Lynch, S.; Oduselu, T.J.; Khan, F.M.; Ayobami, A.; Adnan, F.; Torrents, E.; et al. Phage-Encoded Endolysins. Antibiotics 2021, 10, 124. [Google Scholar] [CrossRef] [PubMed]
- Yan, J.; Mao, J.; Xie, J. Bacteriophage polysaccharide depolymerases and biomedical applications. BioDrugs 2014, 28, 265–274. [Google Scholar] [CrossRef] [PubMed]
- Ha, E.; Son, B.; Ryu, S. Clostridium perfringens virulent bacteriophage CPS2 and its thermostable endolysin lysCPS2. Viruses 2018, 10, 251. [Google Scholar] [CrossRef] [Green Version]
- Plotka, M.; Kapusta, M.; Dorawa, S.; Kaczorowska, A.K.; Kaczorowski, T. Ts2631 endolysin from the extremophilic thermus scotoductus bacteriophage vB_Tsc2631 as an antimicrobial agent against gram-negative multidrug-resistant bacteria. Viruses 2019, 11, 657. [Google Scholar] [CrossRef] [Green Version]
- Pastagia, M.; Schuch, R.; Fischetti, V.A.; Huang, D.B. Lysins: The arrival of pathogen-directed anti-infectives. J. Med. Microbiol. 2013, 62, 1506–1516. [Google Scholar] [CrossRef]
- Abril, A.G.; Carrera, M.; Notario, V.; Sánchez-Pérez, Á.; Villa, T.G. The Use of Bacteriophages in Biotechnology and Recent Insights into Proteomics. Antibiotics 2022, 11, 653. [Google Scholar] [CrossRef]
- Latka, A.; Maciejewska, B.; Majkowska-Skrobek, G.; Briers, Y.; Drulis-Kawa, Z. Bacteriophage-encoded virion-associated enzymes to overcome the carbohydrate barriers during the infection process. Appl. Microbiol. Biotechnol. 2017, 101, 3103–3119. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Scholl, D. Phage Tail-Like Bacteriocins. Annu. Rev. Virol. 2017, 4, 453–467. [Google Scholar] [CrossRef] [PubMed]
- Daw, M.A.; Falkiner, F.R. Bacteriocins: Nature, function and Structure. Micron 1996, 27, 467–479. [Google Scholar] [CrossRef]
- Chen, J.; Zhu, Y.; Yin, M.; Xu, Y.; Liang, X.; Huang, Y.P. Characterization of maltocin S16, a phage tail-like bacteriocin with antibacterial activity against Stenotrophomonas maltophilia and Escherichia coli. J. Appl. Microbiol. 2019, 127, 78–87. [Google Scholar] [CrossRef] [PubMed]
- Morse, S.A.; Jones, B.V.; Lysko, P.G. Pyocin inhibition of Neisseria gonorrhoea: Mechanism of action. Antimicrob. Agents Chemother. 1980, 18, 416–423. [Google Scholar] [CrossRef] [Green Version]
- Lee, G.; Chakraborty, U.; Gebhart, D.; Govoni, G.R.; Zhou, Z.H.; Scholl, D. F-type bacteriocins of Listeria monocytogenes: A new class of phage tail-like structures reveals broad parallel coevolution between tailed bacteriophages and high-molecular-weight bacteriocins. J. Bacteriol. 2016, 198, 2784–2793. [Google Scholar] [CrossRef] [Green Version]
- Tajbakhsh, M.; Karimi, A.; Fallah, F.; Akhavan, M.M. Overview of ribosomal and non-ribosomal antimicrobial peptides produced by Gram positive bacteria. Cell. Mol. Biol. 2017, 6, 20. [Google Scholar] [CrossRef] [PubMed]
- Diep, D.; Nes, I. Ribosomally Synthesized Antibacterial Peptides in Gram Positive Bacteria. Curr. Drug Targets 2005, 3, 107–122. [Google Scholar] [CrossRef]
- Yeaman, M.R.; Yount, N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003, 55, 27–55. [Google Scholar] [CrossRef] [Green Version]
- Kumariya, R.; Kumari, G.; Raiput, Y.S.; Akhtar, N.; Patel, S. Bacteriocins: Classification, synthesis, mechanism of action and resistance development in food spoilage causing bacteria. Microb. Pathog. 2019, 128, 171–177. [Google Scholar] [CrossRef]
- Meade, E.; Slattery, M.A.; Garvey, M. Bacteriocins, Potent Antimicrobial Peptides and the Fight against Multi Drug Resistant Species: Resistance Is Futile? Antibiotics 2020, 9, 32. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gradisteanu Pircalabioru, G.; Popa, L.I.; Marutescu, L.; Gheorghe, I.; Popa, M.; Czobor Barbu, I.; Cristescu, R.; Chifiriuc, M.-C. Bacteriocins in the Era of Antibiotic Resistance: Rising to the Challenge. Pharmaceutics 2021, 13, 196. [Google Scholar] [CrossRef] [PubMed]
- Bierbaum, G.; Sahl, H.-G. Lantibiotics: Mode of Action, Biosynthesis and Bioengineering. Curr. Pharm. Biotechnol. 2009, 10, 2–18. [Google Scholar] [CrossRef] [PubMed]
- Cotter, P.D.; Hill, C.; Ross, R.P. Food microbiology: Bacteriocins: Developing innate immunity for food. Nat. Rev. Microbiol. 2005, 3, 777–788. [Google Scholar] [CrossRef] [PubMed]
- Cintas, L.M.; Casaus, P.; Håvarstein, L.S.; Hernández, P.E.; Nes, I.F. Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum. Appl. Environ. Microbiol. 1997, 63, 4321–4330. [Google Scholar] [CrossRef] [Green Version]
- Nissen-Meyer, J.; Oppegård, C.; Rogne, P.; Haugen, H.S.; Kristiansen, P.E. Structure and mode-of-action of the two-peptide (class-IIb) bacteriocins. Probiotics Antimicrob. Proteins 2010, 2, 52–60. [Google Scholar] [CrossRef] [Green Version]
- Van Belkum, M.J.; Martin-Visscher, L.A.; Vederas, J.C. Structure and genetics of circular bacteriocins. Trends Microbiol. 2011, 19, 411–418. [Google Scholar] [CrossRef]
- Nissen-Meyer, J.; Rogne, P.; Oppegard, C.; Haugen, H.; Kristiansen, P. Structure-Function Relationships of the Non-Lanthionine-Containing Peptide (class II) Bacteriocins Produced by Gram-Positive Bacteria. Curr. Pharm. Biotechnol. 2009, 10, 19–37. [Google Scholar] [CrossRef]
- Heng, N.C.K.; Wescombe, P.A.; Burton, J.P.; Jack, R.W.; Tagg, J.R. The diversity of bacteriocins in Gram-positive bacteria. In Bacteriocins: Ecology and Evolution; Riley, M.A., Chavan, M.A., Eds.; Springer: New York, NY, USA, 2007; pp. 45–92. [Google Scholar]
- Simons, A.; Alhanout, K.; Duval, R.E. Bacteriocins, Antimicrobial Peptides from Bacterial Origin: Overview of Their Biology and Their Impact against Multidrug-Resistant Bacteria. Microorganisms 2020, 8, 639. [Google Scholar] [CrossRef]
- Duquesne, S.; Destoumieux-Garzón, D.; Peduzzi, J.; Rebuffat, S. Microcins, gene-encoded antibacterial peptides from enterobacteria. Nat. Prod. Rep. 2007, 24, 708–734. [Google Scholar] [CrossRef]
- Pons, A.M.; Lanneluc, I.; Cottenceau, G.; Sable, S. New developments in non-post translationally modified microcins. Biochimie 2002, 84, 531–537. [Google Scholar] [CrossRef]
- Cascales, E.; Buchanan, S.K.; Duche, D.; Kleanthous, C.; Lloubes, R.; Postle, K.; Riley, M.; Slatin, S.; Cavard, D. Colicin biology. Microbiol. Mol. Biol. Rev. 2007, 71, 158–229. [Google Scholar] [CrossRef] [Green Version]
- Gillor, O.; Kirkup, B.C.; Riley, M.A. Colicins and microcins: The next generation antimicrobials. Adv. Appl. Microbiol. 2004, 54, 129–146. [Google Scholar] [PubMed]
- Papadakos, G.; Wojdyla, J.A.; Kleanthous, C. Nuclease colicins and their immunity proteins. Q. Rev. Biophys. 2012, 45, 57–103. [Google Scholar] [CrossRef] [PubMed]
- Duclohier, H. Antimicrobial Peptides and Peptaibols, Substitutes for Conventional Antibiotics. Curr. Pharm. Des. 2010, 16, 3212–3223. [Google Scholar] [CrossRef]
- Wu, J.; Gao, B.; Zhu, S. The fungal defensin family enlarged. Pharmaceuticals 2014, 7, 866–880. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Evans, B.S.; Robinson, S.J.; Kelleher, N.L. Surveys of non-ribosomal peptide and polyketide assembly lines in fungi and prospects for their analysis in vitro and in vivo. Fungal Genet. Biol. 2011, 48, 49–61. [Google Scholar] [CrossRef] [Green Version]
- Tyśkiewicz, R.; Nowak, A.; Ozimek, E.; Jaroszuk-Ściseł, J. Trichoderma: The Current Status of Its Application in Agriculture for the Biocontrol of Fungal Phytopathogens and Stimulation of Plant Growth. Int. J. Mol. Sci. 2022, 23, 2329. [Google Scholar] [CrossRef]
- Leitgeb, B.; Szekeres, A.; Manczinger, L.; Vágvölgyi, C.; Kredics, L. The history of Alamethicin: A review of the most extensively studied peptaibol. Chem. Biodivers. 2007, 4, 1027–1051. [Google Scholar] [CrossRef]
- Szekeres, A.; Leiteb, B.; Kredics, L.; Antal, Z.; Hatvani, L.; Manczinger, L.; Vágvölgyi, C. Peptaibols and related peptaibiotics of Trichoderma. Acta Microbiol. Immunol. Hung. 2005, 52, 137–168. [Google Scholar] [CrossRef]
- Hou, X.; Sun, R.; Feng, Y.; Zhang, R.; Zhu, T.; Che, Q.; Zhang, G.; Li, D. Peptaibols: Diversity, bioactivity, and biosynthesis. Eng. Microbiol. 2022, 2, 100026. [Google Scholar] [CrossRef]
- Qi, S.; Gao, B.; Zhu, S. A Fungal Defensin Inhibiting Bacterial Cell-Wall Biosynthesis with Non-Hemolysis and Serum Stability. J. Fungi 2022, 8, 174. [Google Scholar] [CrossRef]
- Schneider, T.; Kruse, T.; Wimmer, R.; Wiedemann, I.; Sass, V.; Pag, U.; Jansen, A.; Nielsen, A.K.; Mygind, P.H.; Raventós, D.S.; et al. Plectasin, a fungal defensin, targets the bacterial cell wall precursor lipid II. Science 2010, 328, 1168–1172. [Google Scholar] [CrossRef] [Green Version]
- Lima, A.M.; Azevedo, M.I.; Sousa, L.M.; Oliveira, N.S.; Andrade, C.R.; Freitas, C.D.; Souza, P.F. Plant antimicrobial peptides: An overview about classification, toxicity and clinical applications. Int. J. Biol. Macromol. 2022, 214, 10–21. [Google Scholar] [CrossRef]
- Goyal, R.K.; Mattoo, A.K. Plant antimicrobial peptides. In Host Defense Peptides and Their Potential as Therapeutic Agents; Epand, R.M., Ed.; Springer: Cham, Switzerland, 2016; pp. 111–136. [Google Scholar]
- Thevissen, K.; Ferket, K.K.A.; François, I.E.J.A.; Cammue, B.P.A. Interactions of antifungal plant defensins with fungal membrane components. Peptides 2003, 24, 1705–1712. [Google Scholar] [CrossRef]
- Paul, M.; Chowdhury, T.; Saha, S. Antimicrobial peptide: A competent tool for plant disease control in mulberry—A review. Vegetos 2022, 1–10. [Google Scholar] [CrossRef]
- Vasilchenko, A.S.; Smirnov, A.N.; Zavriev, S.K.; Grishin, E.V.; Vasilchenko, A.V.; Rogozhin, E.A. Novel thionins from black seed (Nigella sativa L.) demonstrate antimicrobial activity. Int. J. Pept. Res. Ther. 2017, 23, 171–180. [Google Scholar] [CrossRef]
- Moore, S.J.; Leung, C.L.; Cochran, J.R. Knottins: Disulfide-bonded therapeutic and diagnostic peptides. Drug Discov. Today Technol. 2012, 9, e3–e11. [Google Scholar] [CrossRef]
- Taveira, G.B.; Carvalho, A.O.; Rodrigues, R.; Trindade, F.G.; Da Cunha, M.; Gomes, V.M. Thionin-like peptide from Capsicum annuum fruits: Mechanism of action and synergism with fluconazole against Candida species. BMC Microbiol. 2016, 16, 12. [Google Scholar] [CrossRef] [Green Version]
- Taveira, G.B.; Mello, É.O.; Carvalho, A.O.; Regente, M.; Pinedo, M.; de La Canal, L.; Rodrigues, R.; Gomes, V.M. Antimicrobial activity and mechanism of action of a thionin-like peptide from Capsicum annuum fruits and combinatorial treatment with fluconazole against Fusarium solani. Biopolymers 2017, 108, e23008. [Google Scholar] [CrossRef]
- Slavokhotova, A.A.; Shelenkov, A.A.; Andreev, Y.A.; Odintsova, T.I. Hevein-Like Antimicrobial Peptides of Plants. Biochemistry 2017, 82, 1659–1674. [Google Scholar] [CrossRef]
- Odintsova, T.; Shcherbakova, L.; Slezina, M.; Pasechnik, T.; Kartabaeva, B.; Istomina, E.; Dzhavakhiya, V. Hevein-like antimicrobial peptides WAMPs: Structure-function relationship in antifungal activity and sensitization of plant pathogenic fungi to tebuconazole by WAMP-2-derived peptides. Int. J. Mol. Sci. 2020, 21, 7912. [Google Scholar] [CrossRef]
- Kramer, K.J.; Klassen, L.W.; Jones, B.L.; Speirs, R.D.; Kammer, A.E. Toxicity of purothionin and its homologues to the tobacco hornworm, Manduca sexta (L.) (lepidoptera:Sphingidae). Toxicol. Appl. Pharmacol. 1979, 48, 179–183. [Google Scholar] [CrossRef]
- Azmi, S.; Hussain, M.K. Analysis of structures, functions, and transgenicity of phytopeptides defensin and thionin: A review. Beni Suef. Univ. J. Basic Appl. Sci. 2021, 10, 5. [Google Scholar] [CrossRef]
- Gao, B.; Zhu, S. A Fungal Defensin Targets the SARS−CoV−2 Spike Receptor−Binding Domain. J. Fungi 2021, 7, 553. [Google Scholar] [CrossRef]
- dos Santos-Silva, C.A.; Zupin, L.; Oliveira-Lima, M.; Vilela, L.M.B.; Bezerra-Neto, J.P.; Ferreira-Neto, J.R.; Ferreira, J.D.C.; de Oliveira-Silva, R.L.; de Pires, C.J.; Aburjaile, F.F.; et al. Plant Antimicrobial Peptides: State of the Art, In Silico Prediction and Perspectives in the Omics Era. Bioinform. Biol. Insights 2020, 14, 117793222095273. [Google Scholar] [CrossRef]
- Hellinger, R.; Gruber, C.W. Peptide-based protease inhibitors from plants. Drug Discov. Today 2019, 24, 1877–1889. [Google Scholar] [CrossRef]
- Molesini, B.; Treggiari, D.; Dalbeni, A.; Minuz, P.; Pandolfini, T. Plant cystine-knot peptides: Pharmacological perspectives. Br. J. Clin. Pharmacol. 2017, 83, 63–70. [Google Scholar] [CrossRef]
- Postic, G.; Gracy, J.; Périn, C.; Chiche, L.; Gelly, J.-C. KNOTTIN: The database of inhibitor cystine knot scaffold after 10 years, toward a systematic structure modeling. Nucleic Acids Res. 2017, 46, D454–D458. [Google Scholar] [CrossRef] [Green Version]
- Slavokhotova, A.A.; Rogozhin, E.A. Defense Peptides From the α-Hairpinin Family Are Components of Plant Innate Immunity. Front. Plant Sci. 2020, 11, 465. [Google Scholar] [CrossRef]
- Haney, E.F.; Petersen, A.P.; Lau, C.K.; Jing, W.; Storey, D.G.; Vogel, H.J. Mechanism of action of puroindoline derived tryptophan-rich antimicrobial peptides. Biochim. Biophys. Acta (BBA) Biomembr. 2013, 1828, 1802–1813. [Google Scholar] [CrossRef] [Green Version]
- Rogozhin, E.; Ryazantsev, D.; Smirnov, A.; Zavriev, S. Primary Structure Analysis of Antifungal Peptides from Cultivated and Wild Cereals. Plants 2018, 7, 74. [Google Scholar] [CrossRef] [Green Version]
- Su, T.; Han, M.; Cao, D.; Xu, M. Molecular and Biological Properties of Snakins: The Foremost Cysteine-Rich Plant Host Defense Peptides. J. Fungi 2020, 6, 220. [Google Scholar] [CrossRef]
- Yeung, H.; Squire, C.J.; Yosaatmadja, Y.; Panjikar, S.; López, G.; Molina, A.; Baker, E.N.; Harris, P.W.; Brimble, M.A. Protein Structures Very Important Paper Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily. Angew. Chem. 2016, 128, 8062–8065. [Google Scholar] [CrossRef]
- Rodríguez, S.; Mariana, D.; Vega, B.; Dans, P.D.; Pandolfi, V.; Benko-Iseppon, A.M.; Cecchetto, G. Antimicrobial and structural insights of a new snakin-like peptide isolated from Peltophorum dubium (Fabaceae). Amino Acids 2018, 50, 1245–1259. [Google Scholar] [CrossRef]
- Zhang, S.; Wang, X. One new kind of phytohormonal signaling integrator: Up-and-coming GASA family genes. Plant Signal. Behav. 2017, 12, e1226453. [Google Scholar] [CrossRef] [Green Version]
- de Veer, S.J.; Kan, M.-W.; Craik, D.J. Cyclotides: From Structure to Function. Chem. Rev. 2019, 119, 12375–12421. [Google Scholar] [CrossRef]
- Carla Barbosa da Silva Lima, S.; Maria Benko-Iseppon, A.; Pacifico Bezerra Neto, J.; Lindinalva Barbosa Amorim, L.; Ribamar Costa Ferreira Neto, J.; Crovella, S.; Pandolfi, V. Plants defense-related cyclic peptides: Diversity, structure and applications. Curr Protein Pept Sci. 2017, 18, 375–390. [Google Scholar]
- Huang, Y.-H.; Du, Q.; Craik, D.J. Cyclotides: Disulfide-rich peptide toxins in plants. Toxicon 2019, 172, 33–44. [Google Scholar] [CrossRef]
- Selsted, M.E.; Ouellette, A.J. Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 2005, 6, 551–557. [Google Scholar] [CrossRef]
- Niyonsaba, F.; Nagaoka, I.; Ogawa, H.; Okumura, K. Multifunctional antimicrobial proteins and peptides: Natural activators of immune systems. Curr. Pharm. Des. 2009, 15, 2393–2413. [Google Scholar] [CrossRef] [PubMed]
- Ayabe, T.; Satchell, D.P.; Wilson, C.L.; Parks, W.C.; Selsted, M.E.; Ouellette, A.J. Secretion of microbicidal α-defensins by intestinal Paneth cells in response to bacteria. Nat. Immunol. 2000, 1, 113–118. [Google Scholar] [CrossRef] [PubMed]
- Basso, V.; Garcia, A.; Tran, D.Q.; Schaal, J.B.; Tran, P.; Ngole, D.; Aqeel, Y.; Tongaonkar, P.; Ouellette, A.J.; Selsteda, M.E. Fungicidal Potency and Mechanisms of –Defensins against Multidrug-Resistant Candida Species. Antimicrob. Agents Chemother. 2018, 62, e00111-18. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wilmes, M.; Stockem, M.; Bierbaum, G.; Schlag, M.; Götz, F.; Tran, D.Q.; Schaal, J.B.; Ouellette, A.J.; Selsted, M.E.; Sahl, H.-G. Killing of Staphylococci by θ-Defensins Involves Membrane Impairment and Activation of Autolytic Enzymes. Antibiotics 2014, 3, 617–631. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Welkos, S.; Cote, C.K.; Hahn, U.; Shastak, O.; Jedermann, J.; Bozue, J.; Jung, G.; Ruchala, P.; Pratikhya, P.; Tang, T.; et al. Humanized theta-defensins (retrocyclins) enhance macrophage performance and protect mice from experimental anthrax infections. Antimicrob. Agents Chemother. 2011, 55, 4238–4250. [Google Scholar] [CrossRef] [Green Version]
- Hazlett, L.; Wu, M. Defensins in innate immunity. Cell Tissue Res. 2011, 343, 175–188. [Google Scholar] [CrossRef] [PubMed]
- Rowley, A.F.; Powell, A. Invertebrate immune systems specific, quasi-specific, or nonspecific? J. Immunol. 2007, 179, 7209–7214. [Google Scholar] [CrossRef] [Green Version]
- Froy, O. Convergent evolution of invertebrate defensins and nematode antibacterial factors. Trends Microbiol. 2005, 13, 314–319. [Google Scholar] [CrossRef]
- Tassanakajon, A.; Somboonwiwat, K.; Amparyup, P. Sequence diversity and evolution of antimicrobial peptides in invertebrates. Dev. Comp. Immunol. 2015, 48, 324–341. [Google Scholar] [CrossRef]
- Saito, T.; Kawabata, S.I.; Shigenaga, T.; Takayenoki, Y.; Cho, J.; Nakajima, H.; Hirata, M.; Iwanaga, S. A novel big defensin identified in horseshoe crab hemocytes: Isolation, amino acid sequence, and antibacterial activity. J. Biochem. 1995, 117, 1131–1137. [Google Scholar] [CrossRef]
- Ranganathan, S.; Simpson, K.J.; Shaw, D.C.; Nicholas, K.R. The whey acidic protein family: A new signature motif and three-dimensional structure by comparative modeling. J. Mol. Graph. Model. 1999, 17, 106–113. [Google Scholar] [CrossRef]
- Smith, V.J. Phylogeny of whey acidic protein (WAP) four-disulfide core proteins and their role in lower vertebrates and invertebrates. Biochem. Soc. Trans. 2011, 39, 1403–1408. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Masso-Silva, J.A.; Diamond, G. Antimicrobial peptides from fish. Pharmaceuticals 2014, 7, 265–310. [Google Scholar] [CrossRef] [Green Version]
- Nam, B.H.; Moon, J.Y.; Kim, Y.O.; Kong, H.J.; Kim, W.J.; Lee, S.J.; Kim, K.K. Multiple β-defensin isoforms identified in early developmental stages of the teleost Paralichthys olivaceus. Fish Shellfish Immunol. 2010, 28, 267–274. [Google Scholar] [CrossRef] [PubMed]
- Van Harten, R.M.; Van Woudenbergh, E.; Van Dijk, A.; Haagsman, H.P. Cathelicidins: Immunomodulatory Antimicrobials. Vaccines 2018, 6, 63. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Goitsuka, R.; Chen, C.-L.H.; Benyon, L.; Asano, Y.; Kitamura, D.; Cooper, M.D. Chicken cathelicidin-b1, an antimicrobial guardian at the mucosal m cell gateway. Proc. Natl. Acad. Sci. USA 2007, 104, 15063–15068. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Tossi, A.; Scocchi, M.; Zanetti, M.; Storici, P.; Gennaro, R. Pmap-37, a novel antibacterial peptide from pig myeloid cells. Cdna cloning, chemical synthesis and activity. Eur. J. Biochem. 1995, 228, 941–946. [Google Scholar] [CrossRef]
- Veldhuizen, E.J.A.; Scheenstra, M.R.; Tjeerdsma-van Bokhoven, J.L.M.; Coorens, M.; Schneider, V.A.F.; Bikker, F.J.; van Dijk, A.; Haagsman, H.P. Antimicrobial and immunomodulatory activity of pmap-23 derived peptides. Protein Pept. Lett. 2017, 24, 609–616. [Google Scholar] [CrossRef]
- Wessely-Szponder, J.; Majer-Dziedzic, B.; Smolira, A. Analysis of antimicrobial peptides from porcine neutrophils. J. Microbiol. Methods 2010, 83, 8–12. [Google Scholar] [CrossRef]
- Xiao, Y.; Cai, Y.; Bommineni, Y.R.; Fernando, S.C.; Prakash, O.; Gilliland, S.E.; Zhang, G. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J. Biol. Chem. 2006, 281, 2858–2867. [Google Scholar] [CrossRef] [Green Version]
- Liu, Z.-M.; Chen, J.; Lv, Y.-P.; Hu, Z.-H.; Dai, Q.-M.; Fan, X.-L. Molecular characterization of a hepcidin homologue in starry flounder (Platichthys stellatus) and its synergistic interaction with antibiotics. Fish Shellfish Immunol. 2018, 83, 45–51. [Google Scholar] [CrossRef] [PubMed]
- Huang, P.H.; Chen, J.Y.; Kuo, C.M. Three different hepcidins from tilapia, Oreochromis mossambicus: Analysis of their expressions and biological functions. Mol. Immunol. 2007, 44, 1922–1934. [Google Scholar] [CrossRef] [PubMed]
- Hunter, H.N.; Bruce Fulton, D.; Ganz, T.; Vogel, H.J. The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J. Biol. Chem. 2002, 277, 37597–37603. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chaturvedi, P.; Bhat, R.A.H.; Pande, A. Antimicrobial Peptides of Fish: Innocuous Alternatives to Antibiotics. Rev. Aquac. 2020, 12, 85–106. [Google Scholar] [CrossRef]
- Mihailescu, M.; Sorci, M.; Seckute, J.; Silin, V.I.; Hammer, J.; Perrin, P.S., Jr.; Hernandez, J.I.; Smajic, N.; Shrestha, A.; Bogardus, K.A.; et al. structure and function in antimicrobial piscidins: Histidine position, directionality of membrane insertion, and pH-dependent permeabilization. J. Am. Chem. Soc. 2019, 141, 9837–9853. [Google Scholar] [CrossRef] [PubMed]
- Van Hoek, ML Antimicrobial Peptides in Reptiles. Pharmaceuticals 2014, 7, 723–753. [CrossRef] [Green Version]
- Cheng, Y.; Prickett, M.D.; Gutowska, W.; Kuo, R.; Belov, K.; Burt, D.W. Evolution of the avian β-defensin and cathelicidin genes. BMC Evol. Biol. 2015, 15, 188. [Google Scholar] [CrossRef] [Green Version]
- Ageitos, J.M.; Sánchez-Pérez, A.; Calo-Mata, P.; Villa, T.G. Antimicrobial peptides (amps): Ancient compounds that represent novel weapons in the fight against bacteria. Biochem. Pharmacol. 2017, 133, 117–138. [Google Scholar] [CrossRef]
- Wang, J.; Dou, X.; Song, J.; Lyu, Y.; Zhu, X.; Xu, L.; Li, W.; Shan, A. Antimicrobial peptides: Promising alternatives in the post-feeding antibiotic era. Med. Res. Rev. 2019, 39, 831–859. [Google Scholar] [CrossRef]
- Chen, C.H.; Lu, T.K. Development and challenges of antimicrobial peptides for therapeutic applications. Antibiotics 2020, 9, 24. [Google Scholar] [CrossRef] [Green Version]
- Torres, M.D.T.; Sothiselvam, S.; Lu, T.K.; de la Fuente-Nunez, C. Peptide design principles for antimicrobial applications. J. Mol. Biol. 2019, 431, 3547–3567. [Google Scholar] [CrossRef] [PubMed]
- Lei, J.; Sun, L.; Huang, S.; Zhu, C.; Li, P.; He, J.; Mackey, V.; Coy, D.H.; He, Q. The antimicrobial peptides and their potential clinical applications. Am. J. Transl. Res. 2019, 11, 3919–3931. [Google Scholar]
- Luo, Y.; McLean, D.T.F.; Linden, G.J.; McAuley, D.F.; McMullan, R.; Lundy, F.T. The naturally occurring host defense peptide, LL-37, and its truncated mimetics KE-18 and KR-12 have selected biocidal and antibiofilm activities against Candida albicans, Staphylococcus aureus, and Escherichia coli in vitro. Front. Microbiol. 2017, 8, 544. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Phambu, N.; Almarwani, B.; Garcia, A.M.; Hamza, N.S.; Muhsen, A.; Baidoo, J.E.; Sunda-Meya, A. Chain length effect on the structure and stability of antimicrobial peptides of the (RW) series. Biophys. Chem. 2017, 227, 8–13. [Google Scholar] [CrossRef] [PubMed]
- Tripathi, A.K.; Kumari, T.; Harioudh, M.K.; Yadav, P.K.; Kathuria, M.; Shukla, P.K.; Mitra, K.; Ghosh, J.K. Identification of GXXXXG motif in Chrysophsin-1 and its implication in the design of analogs with cell-selective antimicrobial and anti-endotoxin activities. Sci. Rep. 2017, 7, 3384. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wang, J.; Chou, S.; Xu, L.; Zhu, X.; Dong, N.; Shan, A.; Chen, Z. High specific selectivity and Membrane-Active Mechanism of the synthetic centrosymmetric α-helical peptides with Gly-Gly pairs. Sci. Rep. 2015, 5, 1–19. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- De Cândido, E.S.; Cardoso, M.H.S.; Sousa, D.A.; Viana, J.C.; de Oliveira-Júnior, N.G.; Miranda, V.; Franco, O.L. The use of versatile plant antimicrobial peptides in agribusiness and human health. Peptides 2014, 55, 65–78. [Google Scholar] [CrossRef]
- Ilic, N.; Novkovic, M.; Guida, F.; Xhindoli, D.; Benincasa, M.; Tossi, A.; Juretic, D. Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. Biochim. Biophys. Acta 2013, 1828, 1004–1012. [Google Scholar] [CrossRef] [Green Version]
- Leite, N.B.; da Costa, L.C.; Dos Santos Alvares, D.; Dos Santos Cabrera, M.P.; de Souza, B.M.; Palma, M.S.; Ruggiero Neto, J. The effect of acidic residues and amphipathicity on the lytic activities of mastoparan peptides studied by fluorescence and CD spectroscopy. Amino Acids 2011, 40, 91–100. [Google Scholar] [CrossRef]
- Imjongjirak, C.; Amphaiphan, P.; Charoensapsri, W.; Amparyup, P. Characterization and antimicrobial evaluation of SpPR-AMP1, a proline-rich antimicrobial peptide from the mud crab Scylla paramamosain. Dev. Comp. Immunol. 2017, 74, 209–216. [Google Scholar] [CrossRef]
- Li, W.; Tailhades, J.; O’Brien-Simpson, N.M.; Separovic, F.; Otvos, L., Jr.; Hossain, M.A.; Wade, J.D. Proline-rich antimicrobial peptides: Potential therapeutics against antibiotic-resistant bacteria. Amino Acids 2014, 46, 2287–2294. [Google Scholar] [CrossRef] [PubMed]
- Sonderegger, C.; Fizil, Á.; Burtscher, L.; Hajdu, D.; Muñoz, A.; Gáspári, Z.; Read, N.D.; Batta, G.; Marx, F. D19S mutation of the cationic, cysteine-rich protein PAF: Novel insights into its structural dynamics, thermal unfolding and antifungal function. PLoS ONE 2017, 12, e0169920. [Google Scholar]
- Mohanram, H.; Bhattacharjya, S. Cysteine deleted protegrin-1 (cdp-1): Antibacterial activity, outer-membrane disruption and selectivity. Biochim. Biophys. Acta 2014, 1840, 3006–3016. [Google Scholar] [CrossRef] [PubMed]
- Chou, S.L.; Shao, C.X.; Wang, J.J.; Shan, A.S.; Xu, L.; Dong, N.; Li, Z.Y. Short, multiple-stranded β-hairpin peptides have antimicrobial potency with high selectivity and salt resistance. Acta Biomater. 2016, 30, 78–93. [Google Scholar] [CrossRef]
- Lee, E.; Shin, A.; Jeong, K.W.; Jin, B.; Jnawali, H.N.; Shin, S.; Shin, S.Y.; Kim, Y. Role of phenylalanine and valine (10) residues in the antimicrobial activity and cytotoxicity of piscidin-1. PLoS ONE 2014, 9, e114453. [Google Scholar] [CrossRef] [Green Version]
- Tripathi, A.K.; Kumari, T.; Tandon, A.; Sayeed, M.; Afshan, T.; Kathuria, M.; Shukla, P.K.; Mitra, K.; Ghosh, J.K. Selective phenylalanine to proline substitution for improved antimicrobial and anticancer activities of peptides designed on phenylalanine heptad repeat. Acta Biomater. 2017, 57, 170–186. [Google Scholar] [CrossRef]
- Brogden, K.A.; Ackermann, M.; Huttner, K.M. Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial. Antimicrob. Agents Chemother. 1997, 41, 1615–1617. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Mojsoska, B.; Jenssen, H. Peptides and Peptidomimetics for Antimicrobial Drug Design. Pharmaceuticals 2015, 8, 366–415. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Epand, R.M.; Vogel, H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999, 1462, 11–28. [Google Scholar] [CrossRef] [Green Version]
- Padmanabhan, S.; York, E.J.; Stewart, J.M.; Baldwin, R.L. Helix propensities of basic amino acids increase with the length of the side-chain. J. Mol. Biol. 1996, 257, 726–734. [Google Scholar] [CrossRef] [Green Version]
- Pace, C.N.; Scholtz, J.M. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 1998, 75, 422–427. [Google Scholar] [CrossRef] [Green Version]
- Schmidtchen, A.; Pasupuleti, M.; Malmsten, M. Effect of hydrophobic modifications in antimicrobial peptides. Adv. Colloid Interface Sci. 2014, 205, 265–274. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hollmann, A.; Martínez, M.; Noguera, M.E.; Augusto, M.T.; Disalvo, A.; Santos, N.C.; Semorile, L.; Maffía, P.C. Role of amphipathicity and hydrophobicity in the balance between hemolysis and peptide–membrane interactions of three related antimicrobial peptides. Colloids Surf. B Biointerfaces 2016, 141, 528–536. [Google Scholar] [CrossRef] [PubMed]
- Sun, J.; Xia, Y.; Li, D.; Du, Q.; Liang, D. Relationship between peptide structure and antimicrobial activity as studied by de novo designed peptides. Biochim. Biophys. Acta (BBA) Biomembr. 2014, 1838, 2985–2993. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hädicke, A.; Blume, A. Binding of cationic peptides (KX) 4K to DPPG bilayers. Increasing the hydrophobicity of the uncharged amino acid X drives formation of membrane bound β-sheets: A DSC and FT-IR study. Biochim. Biophys. Acta (BBA) Biomembr. 2016, 1858, 1196–1206. [Google Scholar] [CrossRef]
- Wood, S.J.; Park, Y.A.; Kanneganti, N.P.; Mukkisa, H.R.; Crisman, L.L.; Davis, S.E. Modified cysteine-deleted tachyplesin (CDT) analogs as linear antimicrobial peptides: Influence of chain length, positive charge, and hydrophobicity on antimicrobial and hemolytic activity. Int. J. Pept. Res. Ther. 2014, 20, 519–530. [Google Scholar] [CrossRef]
- Wang, J.; Chou, S.; Yang, Z.; Yang, Y.; Wang, Z.; Song, J.; Dou, X.; Shan, A. Combating drug-resistant fungi with novel imperfectly amphipathic palindromic peptides. J. Med. Chem. 2018, 61, 3889–3907. [Google Scholar] [CrossRef]
- Hollmann, A.; Martinez, M.; Maturana, P.; Semorile, L.C.; Maffia, P.C. Antimicrobial peptides: Interaction with model and biological membranes and synergism with chemical antibiotics. Front. Chem. 2018, 6, 204. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Jakel, C.E.; Meschenmoser, K.; Kim, Y.; Weiher, H.; Schmidt-Wolf, I.G. Efficacy of a proapoptotic peptide towards cancer cells. In Vivo 2012, 26, 419–426. [Google Scholar]
- Shai, Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002, 66, 236–248. [Google Scholar] [CrossRef]
- Lee, A.C.-L.; Harris, J.L.; Khanna, K.K.; Hong, J.-H. A Comprehensive Review on Current Advances in Peptide Drug Development and Design. Int. J. Mol. Sci. 2019, 20, 2383. [Google Scholar] [CrossRef] [Green Version]
- Ebenhan, T.; Gheysens, O.; Kruger, H.G.; Zeevaart, J.R.; Sathekge, M.M. Antimicrobial peptides: Their role as infection-selective tracers for molecular imaging. BioMed. Res. Int. 2014, 2014, 867381. [Google Scholar] [CrossRef] [Green Version]
- Fanelli, F.; Cozzi, G.; Raiola, A.; Dini, I.; Mulè, G.; Logrieco, A.F.; Ritieni, A. Raisins and currants as conventional nutraceuticals in Italian market: Natural occurrence of Ochratoxin A. J. Food Sci. 2017, 82, 2306–2312. [Google Scholar] [CrossRef] [PubMed]
- Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415, 389–395. [Google Scholar] [CrossRef] [PubMed]
- McPhee, J.B.; Hancock, R.E. Function and therapeutic potential of host defence peptides. J. Pept. Sci 2005, 11, 677–687. [Google Scholar] [CrossRef]
- Bahar, A.A.; Ren, D. Antimicrobial peptides. Pharmaceuticals 2013, 6, 1543–1575. [Google Scholar] [CrossRef] [Green Version]
- Shai, Y.; Oren, Z. From “carpet” mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 2001, 22, 1629–1641. [Google Scholar] [CrossRef]
- Cruciani, R.A.; Barker, J.L.; Durell, S.R.; Raghunathan, G.; Robert Guy, H.; Zasloff, M.; Stanley, E.F. Magainin 2, a natural antibiotic from frog skin, forms ion channels in lipid bilayer membranes. Eur. J. Pharmacol. Mol. Pharmacol. 1992, 226, 287–296. [Google Scholar] [CrossRef]
- Sengupta, D.; Leontiadou, H.; Mark, A.E.; Marrink, S.J. Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim. Biophys. Acta Biomembr. 2008, 1778, 2308–2317. [Google Scholar] [CrossRef] [Green Version]
- Rozek, A.; Friedrich, C.L.; Hancock, R.E.W. structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 2000, 39, 15765–15774. [Google Scholar] [CrossRef]
- Rapaport, D.; Shai, Y. Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers. J. Biol. Chem. 1991, 266, 23769–23775. [Google Scholar] [CrossRef]
- Yang, L.; Harroun, T.A.; Weiss, T.M.; Ding, L.; Huang, H.W. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 2001, 81, 1475–1485. [Google Scholar] [CrossRef] [Green Version]
- Leontiadou, H.; Mark, A.E.; Marrink, S.J. Antimicrobial peptides in action. J. Am. Chem. Soc. 2006, 128, 12156–12161. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Kumar, P.; Kizhakkedathu, J.N.; Straus, S.K. Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo. Biomolecules 2018, 8, 4. [Google Scholar] [CrossRef] [PubMed]
- Zhang, L.; Rozek, A.; Hancock, R.E.W. Interaction of Cationic Antimicrobial Peptides with Model Membranes. J. Biol. Chem. 2001, 276, 35714–35722. [Google Scholar] [CrossRef] [Green Version]
- Park, C.B.; Kim, M.S.; Kim, S.C. A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem. Biophys. Res. Commun. 1996, 218, 408–413. [Google Scholar] [CrossRef]
- Park, C.B.; Kim, H.S.; Kim, S.C. Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 1998, 244, 253–257. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hancock, R.E.W.; Nijnik, A.; Philpott, D.J. Modulating immunity as a therapy for bacterial infections. Nat. Rev. Microbiol. 2012, 10, 243–254. [Google Scholar] [CrossRef] [PubMed]
- Yeung, A.T.; Gellatly, S.L.; Hancock, R.E. Multifunctional cationic host defence peptides and their clinical applications. Cell Mol Life Sci 2011, 68, 2161–2176. [Google Scholar] [CrossRef]
- Hilchie, A.L.; Wuerth, K.; Hancock, R.E.W. Immune modulation by multifaceted cationic host defense (antimicrobial) peptides. Nat. Chem. Biol. 2013, 9, 761–768. [Google Scholar] [CrossRef]
- Lai, Y.; Gallo, R.L. AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009, 30, 131–141. [Google Scholar] [CrossRef] [Green Version]
- Jiao, K.; Gao, J.; Zhou, T.; Yu, J.; Song, H.; Wei, Y.; Gao, X. Isolation and purification of a novel antimicrobial peptide from Porphyra yezoensis. J. Food Biochem. 2019, 43, e12864. [Google Scholar] [CrossRef] [PubMed]
- Keymanesh, K.; Soltani, S.; Sardari, S. Application of antimicrobial peptides in agriculture and food industry. World J. Microbiol. Biotechnol. 2009, 25, 933–944. [Google Scholar] [CrossRef]
- Naghmouchi, K.; Belguesmia, Y.; Bendali, F.; Spano, G.; Seal, B.S.; Drider, D. Lactobacillus fermentum: A bacterial species with potential for food preservation and biomedical applications. Crit. Rev. Food Sci. Nutr. 2019, 1, 3387–3399. [Google Scholar] [CrossRef] [PubMed]
- Schmitt, P.; Rosa, R.D.; Destoumieux-Garzon, D. An intimate link between antimicrobial peptide sequence diversity and binding to essential components of bacterial membranes. Biochim. Biophys. Acta Biomembr. 2016, 1858, 958–970. [Google Scholar] [CrossRef]
- Lima, K.O.; da Costa de Quadros, C.; Rocha, M.d.; Jocelino Gomes de Lacerda, J.T.; Juliano, M.A.; Dias, M.; Mendes, M.A.; Prentice, C. Bioactivity and bioaccessibility of protein hydrolyzates from industrial byproducts of Stripped weakfish (Cynoscion guatucupa). LWT 2019, 111, 408–413. [Google Scholar] [CrossRef]
- Liu, Y.; Du, Q.; Ma, C.; Xi, X.; Wang, L.; Zhou, M.; Burrows, J.F.; Chen, T.; Wang, H. Structure–activity relationship of an antimicrobial peptide, Phylloseptin-PHa: Balance of hydrophobicity and charge determines the selectivity of bioactivities. Drug Des. Devel. Ther. 2019, 13, 447–458. [Google Scholar] [CrossRef] [Green Version]
- Gddoa Al-sahlany, S.T.; Altemimi, A.B.; Abd Al Manhel, A.J.; Niamah, A.K.; Lakhssasi, N.; Ibrahim, S.A. Purification et bioactive peptide with antimicrobial properties produced by Saccharomyces cerevisiae. Foods 2020, 9, 324. [Google Scholar] [CrossRef] [Green Version]
- Tavano, O.L. Protein hydrolysis using proteases: An important tool for food biotechnology. J. Mol. Catal. B Enzym. 2013, 90, 1–11. [Google Scholar] [CrossRef]
- Mao, Y.; Niu, S.; Xu, X.; Wang, J.; Su, Y.; Wu, Y.; Zhong, S. The effect of an adding histidine on biological activity and stability of pc-pis from Pseudosciaena crocea. PLoS ONE 2013, 8, e83268. [Google Scholar] [CrossRef] [Green Version]
- Shruti, S.R.; Rajasekaran, R. Identification of protegrin-1 as a stable and nontoxic scaffold among protegrin family—A computational approach. J. Biomol. Struct. Dyn. 2019, 37, 2430–2439. [Google Scholar] [CrossRef]
- Van Lancker, F.; Adams, A.; De Kimpe, N. Chemical modifications of peptides and their impact on food properties. Chem. Rev. 2011, 111, 7876–7903. [Google Scholar] [CrossRef] [PubMed]
- Berardo, A.; De Maere, H.; Stavropoulou, D.A.; Rysman, T.; Leroy, F.; De Smet, S. Effect of sodium ascorbate and sodium nitrite on protein and lipid oxidation in dry fermented sausages. Meat Sci. 2016, 121, 359–364. [Google Scholar] [CrossRef] [PubMed]
- Peña-Egido, M.J.; García-Alonso, B.; García-Moreno, C. S-sulfonate contents in raw and cooked meat products. JAFC 2005, 53, 4198–4201. [Google Scholar] [CrossRef] [PubMed]
- Sun, X.; Acquah, C.; Aluko, R.E.; Udenigwe, C.C. Considering food matrix and gastrointestinal effects in enhancing bioactive peptide absorption and bioavailability. J. Funct. Foods 2020, 64, 103680. [Google Scholar] [CrossRef]
- Sarabandi, K.; Gharehbeglou, P.; Jafari, S.M. Spray-drying encapsulation of protein hydrolysates and bioactive peptides: Opportunities and challenges. Dry. Technol. 2020, 38, 577–595. [Google Scholar] [CrossRef]
- Yekta, M.M.; Rezaei, M.; Nouri, L.; Azizi, M.H.; Jabbari, M.; Eş, I.; Khaneghah, A.M. Antimicrobial and antioxidant properties of burgers with quinoa peptide-loaded nanoliposomes. J. Food Saf. 2020, 40, e12753. [Google Scholar] [CrossRef]
- Soto, K.M.; Hernandez-Iturriaga, M.; Loarca-Pina, G.; Luna-Barcenas, G.; Gomez-Aldapa, C.A.; Mendoza, S. Stable nisin food-grade electrospun fibers. J. Food Sci. Technol. 2016, 53, 3787–3794. [Google Scholar] [CrossRef] [Green Version]
- Wu, X.; Wei, P.H.; Zhu, X.; Wirth, M.J.; Bhunia, A.; Narsimhan, G. Effect of immobilization on the antimicrobial activity of a cysteine-terminated antimicrobial Peptide Cecropin P1 tethered to silica nanoparticle against E. coli O157:H7 EDL. Colloids Surf. B Biointerfaces 2017, 156, 305–312. [Google Scholar] [CrossRef]
- Yi, L.; Qi, T.; Ma, J.; Zeng, K. Genome and metabolites analysis reveal insights into control of foodborne pathogens in fresh-cut fruits by Lactobacillus pentosus MS031 isolated from Chinese sichuan paocai. Postharvest Biol. Technol. 2020, 164, 111150. [Google Scholar] [CrossRef]
- Tenea, G.N.; Pozo, T.D. Antimicrobial peptides from Lactobacillus plantarum UTNGt2 prevent harmful bacteria growth on fresh tomatoes. J. Microbiol. Biotechnol. 2019, 29, 1553–1560. [Google Scholar] [CrossRef]
- Gogliettino, M.; Balestrieri, M.; Ambrosio, R.L.; Anastasio, A.; Smaldone, G.; Proroga, Y.T.R.; Moretta, R.; Rea, I.; De Stefano, L.; Agrillo, B.; et al. Extending the Shelf-Life of Meat and Dairy Products via PET-Modified Packaging Activated with the Antimicrobial Peptide MTP1. Front. Microbiol. 2020, 10, 2963. [Google Scholar] [CrossRef] [PubMed]
- Dos Santos Pires, A.C.; De Ferreira Soares, N.F.; De Andrade, N.J.; Mendes Da Silva, L.H.; Peruch Camilloto, G.; Campos Bernardes, P. Development and evaluation of active packaging for sliced mozzarella preservation. Packag. Technol. Sci. 2008, 21, 375–383. [Google Scholar] [CrossRef]
- Da Rocha, M.; Alemán, A.; Romani, V.P.; López-Caballero, M.E.; Gómez-Guillén, M.C.; Montero, P.; Prentice, C. Effects of agar films incorporated with fish protein hydrolysate or clove essential oil on flounder (Paralichthys orbignyanus) fillets shelf-life. Food Hydrocoll. 2018, 81, 351–363. [Google Scholar] [CrossRef]
- Neetoo, H. Use of nisin-coated plastic films to control Listeria monocytogenes on vacuum-packaged cold-smoked salmon. Int. J. Food Microbiol. 2008, 122, 8–15. [Google Scholar] [CrossRef]
- Luo, L.; Wu, Y.; Liu, C.; Zou, Y.; Huang, L.; Liang, Y.; Ren, J.; Liu, Y.; Lin, Q. Elaboration and characterization of curcumin-loaded soy soluble polysaccharide (SSPS)-based nanocarriers mediated by antimicrobial peptide nisin. Food Chem. 2021, 336, 127669. [Google Scholar] [CrossRef] [PubMed]
- Zohri, M.; Shafiee, M.; Ismaeil, A. A comparative study between the antibacterial effect of nisin and nisin-loaded chitosan/alginate nanoparticles on the growth of Staphylococcus aureus in raw and pasteurized milk samples. Probiotics Antimicrob. Proteins 2010, 2, 258–266. [Google Scholar] [CrossRef]
- Piras, A.M.; Maisetta, G.; Sandreschi, S.; Gazzarri, M.; Bartoli, C.; Grassi, L.; Esin, S.; Chiellini, F.; Batoni, G. Chitosan nanoparticles loaded with the antimicrobial peptide temporin B exert a long-term antibacterial activity in vitro against clinical isolates of Staphylococcus epidermidis. Front. Microbiol. 2015, 6, 372. [Google Scholar] [CrossRef] [Green Version]
- Jiang, Y.; Sun, J.; Yin, Z.; Li, H. Evaluation of antioxidant peptides generated from Jiuzao (residue after Baijiu distillation) protein hydrolysates and their effect of enhancing healthy value of Chinese Baijiu. Soc. Chem. Ind. 2019, 100, 59–73. [Google Scholar] [CrossRef]
- Najafian, L.; Babji, A.S. Purification and Identification of Antioxidant Peptides from Fermented Fish Sauce (Budu). J. Aquat. Food Prod. Technol. 2018, 8850, 14–24. [Google Scholar] [CrossRef]
- Wu, D.; Sun, N.; Ding, J.; Zhu, B.; Lin, S. Evaluation and structure-activity relationship analysis of antioxidant shrimp peptides. Food Funct. 2019, 10, 5605–5615. [Google Scholar] [CrossRef]
- Marqus, S.; Pirogova, E.; Piva, T.J. Evaluation of the use of therapeutic peptides for cancer treatment. J. Biomed. Sci. 2017, 24, 21. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Boohaker, R.J.; Lee, M.W.; Vishnubhotla, P.; Perez, J.M.; Khaled, A.R. The use of therapeutic peptides to target and to kill cancer cells. Curr. Med. Chem. 2012, 19, 3794–3804. [Google Scholar] [CrossRef] [PubMed]
- McGregor, D.P. Discovering and improving novel peptide therapeutics. Curr. Opin. Pharmacol. 2008, 8, 616–619. [Google Scholar] [CrossRef] [PubMed]
- Moretta, A.; Scieuzo, C.; Petrone, A.M.; Salvia, R.; Manniello, M.D.; Franco, A.; Lucchetti, D.; Vassallo, A.; Vogel, H.; Sgambato, A.; et al. Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields. Front. Cell. Infect. Microbiol. 2021, 11, 668632. [Google Scholar] [CrossRef]
- Di Grazia, A.; Cappiello, F.; Cohen, H.; Casciaro, B.; Luca, V.; Pini, A.; Di, Y.P.; Shai, Y.; Mangoni, M.L. d-Amino acids incorporation in the frog skin-derived peptide esculentin-1a(1–21)NH2 is beneficial for its multiple functions. Amino Acids 2015, 47, 2505–2519. [Google Scholar] [CrossRef]
- Cappiello, F.; Di Grazia, A.; Segev-Zarko, L.A.; Scali, S.; Ferrera, L.; Galietta, L.; Pini, A.; Shai, Y.; Di, Y.P.; Mangoni, M.L. Esculentin-1a-derived peptides promote clearance of Pseudomonas aeruginosa internalized in bronchial cells of cystic fibrosis patients and lung cell migration: Biochemical properties and a plausible mode of action. Antimicrob. Agents Chemother. 2016, 60, 7252–7262. [Google Scholar] [CrossRef] [Green Version]
- Pero, R.; Brancaccio, M.; Mennitti, C.; Gentile, L.; Franco, A.; Laneri, S.; De Biasi, M.G.; Pagliuca, C.; Colicchio, R.; Salvatore, P.; et al. HNP-1 and HBD-1 as Biomarkers for the Immune Systems of Elite Basketball Athletes. Antibiotics 2020, 9, 306. [Google Scholar] [CrossRef]
- Zhang, P.; Chang, C.; Liu, H.; Li, B.; Yan, Q.; Jiang, Z. Identification of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten hydrolysate by the protease of Pseudomonas aeruginosa. J. Funct. Foods 2020, 65, 103751. [Google Scholar] [CrossRef]
- Wu, C.; Mohammadmoradi, S.; Chen, J.Z.; Sawada, H.; Daugherty, A.; Lu, H.S. Renin-Angiotensin System and Cardiovascular Functions. Arterosclerosis. Thromb. Vasc. Biol. 2018, 38, 108–116. [Google Scholar] [CrossRef] [Green Version]
- Martinez-Villaluenga, C.; Rupasinghe, S.G.; Schuler, M.A.; Gonzalez de Mejia, E. Peptides from purified soybean beta-conglycinin inhibit fatty acid synthase by interaction with the thioesterase catalytic domain. FEBS J. 2010, 277, 1481–1493. [Google Scholar] [CrossRef]
- Hendrikx, T.; Schnabl, B. Antimicrobial proteins: Intestinal guards to protect against liver disease. J. Gastroenterol. 2019, 54, 209–217. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- McCann, K.B.; Lee, A.; Wan, J.; Roginski, H.; Coventry, M.J. The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures. J. Appl. Microbiol. 2003, 95, 1026–1033. [Google Scholar] [CrossRef] [PubMed]
- Pietrantoni, A.; Ammendolia, M.G.; Tinari, A.; Siciliano, R.; Valenti, P.; Superti, F. Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection. Antivir. Res. 2006, 69, 98–106. [Google Scholar] [CrossRef] [PubMed]
- Belaid, A.; Aouni, M.; Khelifa, R.; Trabelsi, A.; Jemmali, M.; Hani, K. In vitro antiviral activity of dermaseptins against herpes simplex virus type 1. J. Med. Virol. 2002, 66, 229–234. [Google Scholar] [CrossRef]
- Mettenleiter, T.C. Brief overview on cellular virus receptors. Virus Res. 2002, 82, 3–8. [Google Scholar] [CrossRef]
- Elnagdy, S.; AlKhazindar, M. The Potential of Antimicrobial Peptides as an Antiviral Therapy against COVID-19. ACS Pharm. Transl. Sci. 2020, 3, 780–782. [Google Scholar] [CrossRef]
- Kudryashova, E.; Zani, A.; Vilmen, G.; Sharma, A.; Lu, W.; Yount, J.S.; Kudryashov, D.S. SARS-CoV-2 incativation by human defensin HNP1 and retrocyclin RC-101. bioRxiv 2021. [Google Scholar] [CrossRef]
- Brancaccio, M.; Mennitti, C.; Calvanese, M.; Gentile, A.; Musto, R.; Gaudiello, G.; Scamardella, G.; Terracciano, D.; Frisso, G.; Pero, R.; et al. Diagnostic and Therapeutic Potential for HNP-1, HBD-1 and HBD-4 in Pregnant Women with COVID-19. Int. J. Mol. Sci. 2022, 23, 3450. [Google Scholar] [CrossRef]
- Laneri, S.; Brancaccio, M.; Mennitti, C.; De Biasi, M.G.; Pero, M.E.; Pisanelli, G.; Scudiero, O.; Pero, R. Antimicrobial Peptides and Physical Activity: A Great Hope against COVID 19. Microorganisms 2021, 9, 1415. [Google Scholar] [CrossRef]
- Chianese, A.; Zannella, C.; Monti, A.; De Filippis, A.; Doti, N.; Franci, G.; Galdiero, M. The Broad-Spectrum Antiviral Potential of the Amphibian Peptide AR-23. Int. J. Mol. Sci. 2022, 23, 883. [Google Scholar] [CrossRef]
- Zannella, C.; Chianese, A.; Palomba, L.; Marcocci, M.E.; Bellavita, R.; Merlino, F.; Grieco, P.; Folliero, V.; De Filippis, A.; Mangoni, M.; et al. Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs. Int. J. Mol. Sci. 2022, 23, 2060. [Google Scholar] [CrossRef] [PubMed]
- Ramos, R.; Silva, J.P.; Rodrigues, A.C.; Costa, R.; Guardao, L.; Schmitt, F.; Soares, R.; Vilanova, M.; Domingues, L.; Gama, M. Wound healing activity of the human antimicrobial peptide ll37. Peptides 2011, 32, 1469–1476. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Simanski, M.; Gläser, R.; Harder, J. Human skin engages different epidermal layers to provide distinct innate defense mechanisms. Exper. Dermat. 2014, 23, 230–231. [Google Scholar] [CrossRef]
- Schröder, J.M.; Harder, J. Antimicrobial skin peptides and proteins. Cell. Mol. Life Sci. 2006, 63, 469–486. [Google Scholar] [CrossRef] [PubMed]
- Mangoni, M.L.; McDermott, A.M.; Zasloff, M. Antimicrobial peptides and wound healing: Biological and therapeutic considerations. Exp. Dermatol. 2016, 25, 167–173. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- El-Seedi, H.; Abd El-Wahed, A.; Yosri, N.; Musharraf, S.G.; Chen, L.; Moustafa, M.; Zou, X.; Al-Mousawi, S.; Guo, Z.; Khatib, A.; et al. Antimicrobial Properties of Apis mellifera’s Bee Venom. Toxins 2020, 12, 451. [Google Scholar] [CrossRef]
Animals | AMPs |
---|---|
Mammalians | cathelicidins defensins (α-, β-, and θ-defensins; θ-defensins are not expressed in adult humans) platelet antimicrobial proteins dermicidins hepcidins |
Reptiles | defensins (α, β-, and θ-defensins) cathelicidins |
Fish | β-defensins cathelicidins hepicidins (HAMP1 and HAMP2) histone-derived peptides piscidins (piscidins 1–7) |
Amphibians | magainins cancrins |
Crustaceans | crustins |
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Dini, I.; De Biasi, M.-G.; Mancusi, A. An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources. Antibiotics 2022, 11, 1483. https://doi.org/10.3390/antibiotics11111483
Dini I, De Biasi M-G, Mancusi A. An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources. Antibiotics. 2022; 11(11):1483. https://doi.org/10.3390/antibiotics11111483
Chicago/Turabian StyleDini, Irene, Margherita-Gabriella De Biasi, and Andrea Mancusi. 2022. "An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources" Antibiotics 11, no. 11: 1483. https://doi.org/10.3390/antibiotics11111483