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Antibiotics
Special Issues
Design, Modification and Application of Antimicrobial Peptides
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Design, Modification and Application of Antimicrobial Peptides

A special issue of Antibiotics (ISSN 2079-6382). This special issue belongs to the section "Antimicrobial Peptides".

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 11065

Special Issue Editors

Dr. Sónia Gonçalves

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Guest Editor
Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisbon, Portugal
Interests: antimicrobial peptides; antimicrobial biomaterials
Special Issues, Collections and Topics in MDPI journals
Dr. Claudia Monteiro

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Guest Editor
Instituto de Investigação e Inovação em Saúde, Universidade do Porto, 4050-313 Porto, Portugal
Interests: antimicrobial peptides; antimicrobial compounds; biofilms; biomaterials
Special Issues, Collections and Topics in MDPI journals
Dr. Ana Margarida Pereira

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Guest Editor
CBMA (Centre of Molecular and Environmental Biology), Department of Biology, Campus de Gualtar, University of Minho, 4710-057 Braga, Portugal
Interests: antimicrobial resistance; antimicrobial peptides; antimicrobial biomaterials
Dr. Pedro Soares-Castro

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Guest Editor
Instituto de Medicina Molecular João Lobo Antunes – Faculty of Medicine, University of Lisbon, 1300-477 Lisbon, Portugal
Interests: microbial functional genomics; cell-factories; bacterial secondary metabolism; prokaryotic synthetic biology; antimicrobial compounds; multidrug resistance
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Globally, antibiotic resistance continues to pose a well-recognized problem, being considered one of the top 10 global public health threats by the World Health Organization (WHO) as it continues to rise to alarmingly high levels worldwide. Prompted by the misuse and overuse of antibiotics in humans, livestock, and agriculture practices, new resistance mechanisms are emerging and spreading among not only nosocomial but also community-acquired pathogens, leading common infections becoming increasingly difficult or even impossible to treat as these antimicrobial agents become less effective.

Due to their broad-spectrum activity, cell selectivity, and reduced likelihood of inducing bacterial resistance, antimicrobial peptides (AMPs) represent a promising alternative to classical antibiotics in fields such as agriculture, the food industry, pharmacology, and medicine. Limitations in terms of the potential high-cost production, toxicity, and stability of AMPs can be overcome by rational design and modification of these molecules, at the same time enhancing their activity against drug-resistant pathogens and expanding their applicability.

With this Special Issue, we hope to present an updated overview of the multidisciplinary research regarding the production, modification, or de novo design of AMPs and their wide range of potential applications in several fields. All types of submissions (original research papers, short communications, reviews, case reports, in silico designs, etc.) related to these topics are welcomed.

Dr. Sónia Gonçalves
Dr. Claudia Monteiro
Dr. Ana Margarida Pereira
Dr. Pedro Soares-Castro
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antibiotics is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • peptide design
  • natural and synthetic AMPs
  • structural modification
  • antimicrobial peptides (AMPs)
  • multidrug resistant bacteria
  • drug optimization
  • therapeutic applications
  • AMP–membrane interaction
  • methodologies for the characterization of AMPs
  • computational modeling

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Published Papers (5 papers)

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Research

22 pages, 7197 KiB  
Article
Progressive Design of a Ranatuerin-2 Peptide from Amolops wuyiensis: Enhancement of Bioactivity and In Vivo Efficacy
by Aifang Yao, Tianxing Liu, Yuhai Cai, Siqi Zhou, Xiaoling Chen, Mei Zhou, Chengbang Ma, Tianbao Chen, Chris Shaw and Lei Wang
Antibiotics 2024, 13(1), 5; https://doi.org/10.3390/antibiotics13010005 - 19 Dec 2023
Cited by 3 | Viewed by 1645
Abstract
Antimicrobial peptides (AMPs) that exert multiple functions are considered promising candidates to combat the bacterial drug resistance crisis. Nowadays, targeted peptide modification has been widely recognised to improve biological activity and make up for deficiencies in clinical applications such as toxicity. In this [...] Read more.
Antimicrobial peptides (AMPs) that exert multiple functions are considered promising candidates to combat the bacterial drug resistance crisis. Nowadays, targeted peptide modification has been widely recognised to improve biological activity and make up for deficiencies in clinical applications such as toxicity. In this study, a helix-loop peptide was isolated and identified from the skin secretion of the Wuyi torrent frog Amolops wuyiensis, namely, ranatuerin-2-AW (R2AW) (GFMDTAKNVAKNVAATLLDKLKCKITGGC). Target modifications were made to R2AW to study the structure–activity relationships and to optimise its bioactivities. Five analogues were progressively designed via residue substitution and truncation and the antibacterial and anticancer activities were evaluated. We found that the serine-substitution and cyclic-domain-deletion products showed similar antibacterial activity to the natural peptide R2AW, implying that the disulphide bridge and Rana box were dispensable for the antibacterial activity of ranatuerin-2 peptides. Notably, the cationicity- and hydrophobicity-enhanced variant, [Lys4,19, Leu20]R2AW(1-22)-NH2, exhibited significantly optimised antibacterial and anticancer activities. Additionally, it killed bacteria by membrane disruption at a highly efficient rate. Moreover, [Lys4,19, Leu20]R2AW(1-22)-NH2 exerted potential in vivo efficacy in a methicillin-resistant Staphylococcus aureus (MRSA)-infected waxworm model. Overall, this study demonstrated some rational design ideas for optimising the dual antibacterial and anticancer activities of ranatuerin-2 peptides and it proposes [Lys4,19, Leu20]R2AW(1-22)-NH2 as an appealing candidate for therapeutic development. Full article
(This article belongs to the Special Issue Design, Modification and Application of Antimicrobial Peptides)
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18 pages, 3389 KiB  
Article
Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria
by Denise Meinberger, Marco G. Drexelius, Joshua Grabeck, Gabriele Hermes, Annika Roth, Dzemal Elezagic, Ines Neundorf, Thomas Streichert and Andreas R. Klatt
Antibiotics 2023, 12(10), 1532; https://doi.org/10.3390/antibiotics12101532 - 11 Oct 2023
Cited by 3 | Viewed by 1950
Abstract
Antimicrobial peptides (AMPs) represent a promising alternative to conventional antibiotics. Sequence changes can significantly improve the therapeutic properties of antimicrobial peptides. In our study, we apply different sequence modifications to enhance the performance of the CLEC3A-derived AMPs HT-16 and HT-47. We truncated their [...] Read more.
Antimicrobial peptides (AMPs) represent a promising alternative to conventional antibiotics. Sequence changes can significantly improve the therapeutic properties of antimicrobial peptides. In our study, we apply different sequence modifications to enhance the performance of the CLEC3A-derived AMPs HT-16 and HT-47. We truncated their sequences, inserting a triple-glycine linker, adding an N-terminal tryptophan residue, and generating a D-amino acid variant, resulting in the generation of seven new peptides. We investigated their antimicrobial activity against gram-positive and gram-negative bacteria, their cytotoxicity to murine cells, and the biostability of the modified peptides in serum. We identified a novel antimicrobial peptide, WRK-30, with enhanced antimicrobial potency against S. aureus and MRSA. Additionally, WRK-30 was less cytotoxic to eukaryotic cells, allowing its application in higher concentrations in an in vivo setting. In conclusion, we identified a novel CLEC3A-derived antimicrobial peptide WRK-30 with significantly improved therapeutic properties and the potential to widen the repertoire of conventional antibiotics. Full article
(This article belongs to the Special Issue Design, Modification and Application of Antimicrobial Peptides)
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13 pages, 1465 KiB  
Article
Engineering and Purification of Microcin C7 Variants Resistant to Trypsin and Analysis of Their Biological Activity
by Guangxin Yang, Lijun Shang, Lu Liu, Zeqiang Li, Xiangfang Zeng, Xiuliang Ding, Jinxiu Huang, Shiyan Qiao and Haitao Yu
Antibiotics 2023, 12(9), 1346; https://doi.org/10.3390/antibiotics12091346 - 22 Aug 2023
Cited by 1 | Viewed by 1639
Abstract
Microcin C7 (McC) as a viable form of antimicrobial has gained substantial attention due to its distinctive antimicrobial activity, by targeting aspartyl tRNA synthetase. McC can be a potential solution against pathogenic microbial infections in the postantibiotic era. However, considering that degradation by [...] Read more.
Microcin C7 (McC) as a viable form of antimicrobial has gained substantial attention due to its distinctive antimicrobial activity, by targeting aspartyl tRNA synthetase. McC can be a potential solution against pathogenic microbial infections in the postantibiotic era. However, considering that degradation by digestive enzymes can disrupt the function of this peptide in the gastrointestinal tract, in this study, we attempt to design McC variants to overcome several barriers that may affect its stability and biological activity. The mccA gene encoding the McC peptide precursor was mutated and 12 new McC variants with trypsin resistance were found. The Yej+rimL− strain was used as an indicator to determine the minimum inhibitory concentrations (MICs). The results showed that three variants, including R2A, R2T and R2Q, among 12 variants formed by the replacement of the second arginine of the McC peptide with different amino acids, were resistant to trypsin and had an outstanding antimicrobial ability, with MIC values of 12.5, 25, and 25 μg/mL, respectively. Taken together, our findings show that the engineering of the site-directed mutagenesis of McC significantly enhances McC trypsin resistance and maintains a great antimicrobial activity. Full article
(This article belongs to the Special Issue Design, Modification and Application of Antimicrobial Peptides)
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28 pages, 4993 KiB  
Article
Complex Networks Analyses of Antibiofilm Peptides: An Emerging Tool for Next-Generation Antimicrobials’ Discovery
by Guillermin Agüero-Chapin, Agostinho Antunes, José R. Mora, Noel Pérez, Ernesto Contreras-Torres, José R. Valdes-Martini, Felix Martinez-Rios, Cesar H. Zambrano and Yovani Marrero-Ponce
Antibiotics 2023, 12(4), 747; https://doi.org/10.3390/antibiotics12040747 - 13 Apr 2023
Cited by 5 | Viewed by 2359
Abstract
Microbial biofilms cause several environmental and industrial issues, even affecting human health. Although they have long represented a threat due to their resistance to antibiotics, there are currently no approved antibiofilm agents for clinical treatments. The multi-functionality of antimicrobial peptides (AMPs), including their [...] Read more.
Microbial biofilms cause several environmental and industrial issues, even affecting human health. Although they have long represented a threat due to their resistance to antibiotics, there are currently no approved antibiofilm agents for clinical treatments. The multi-functionality of antimicrobial peptides (AMPs), including their antibiofilm activity and their potential to target multiple microbes, has motivated the synthesis of AMPs and their relatives for developing antibiofilm agents for clinical purposes. Antibiofilm peptides (ABFPs) have been organized in databases that have allowed the building of prediction tools which have assisted in the discovery/design of new antibiofilm agents. However, the complex network approach has not yet been explored as an assistant tool for this aim. Herein, a kind of similarity network called the half-space proximal network (HSPN) is applied to represent/analyze the chemical space of ABFPs, aiming to identify privileged scaffolds for the development of next-generation antimicrobials that are able to target both planktonic and biofilm microbial forms. Such analyses also considered the metadata associated with the ABFPs, such as origin, other activities, targets, etc., in which the relationships were projected by multilayer networks called metadata networks (METNs). From the complex networks’ mining, a reduced but informative set of 66 ABFPs was extracted, representing the original antibiofilm space. This subset contained the most central to atypical ABFPs, some of them having the desired properties for developing next-generation antimicrobials. Therefore, this subset is advisable for assisting the search for/design of both new antibiofilms and antimicrobial agents. The provided ABFP motifs list, discovered within the HSPN communities, is also useful for the same purpose. Full article
(This article belongs to the Special Issue Design, Modification and Application of Antimicrobial Peptides)
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16 pages, 6910 KiB  
Article
Design of Antimicrobial Peptides with Cell-Selective Activity and Membrane-Acting Mechanism against Drug-Resistant Bacteria
by Seong-Cheol Park, Hyosuk Son, Young-Min Kim, Jong-Kook Lee, Soyoung Park, Hye Song Lim, Jung Ro Lee and Mi-Kyeong Jang
Antibiotics 2022, 11(11), 1619; https://doi.org/10.3390/antibiotics11111619 - 13 Nov 2022
Cited by 12 | Viewed by 2429
Abstract
Antimicrobial peptides (AMPs) can combat drug-resistant bacteria with their unique membrane-disruptive mechanisms. This study aimed to investigate the antibacterial effects of several membrane-acting peptides with amphipathic structures and positional alterations of two tryptophan residues. The synthetic peptides exhibited potent antibacterial activities in a [...] Read more.
Antimicrobial peptides (AMPs) can combat drug-resistant bacteria with their unique membrane-disruptive mechanisms. This study aimed to investigate the antibacterial effects of several membrane-acting peptides with amphipathic structures and positional alterations of two tryptophan residues. The synthetic peptides exhibited potent antibacterial activities in a length-dependent manner against various pathogenic drug-resistant and susceptible bacteria. In particular, the location of tryptophan near the N-terminus of AMPs simultaneously increases their antibacterial activity and toxicity. Furthermore, the growth inhibition mechanisms of these newly designed peptides involve cell penetration and destabilization of the cell membrane. These findings provide new insights into the design of peptides as antimicrobial agents and suggest that these peptides can be used as substitutes for conventional antibiotics. Full article
(This article belongs to the Special Issue Design, Modification and Application of Antimicrobial Peptides)
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