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Biomolecules
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Nature Inspired Peptides in Medical Sciences
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Nature Inspired Peptides in Medical Sciences

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Cellular Biochemistry".

Deadline for manuscript submissions: closed (15 December 2022) | Viewed by 31386

Special Issue Editor

Prof. Dr. Zofia Urbanczyk-Lipkowska

E-Mail Website
Guest Editor
Institute of Organic Chemistry, Polish Academy of Sciences, Kasprzaka Str. 44/52, 01-224 Warsaw, Poland
Interests: bioinspired peptide dendrimers, dendrimer chemistry; nanomolecular antioxidants and free radical scavengers; chiral coordination polymers
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Biomolecules invites submissions to a Special Issue focused on the chemistry, biology, and medical application of natural peptides and their mimetics in recognition of Nature’s remarkable inspiration for gaining new ideas for future medicine.

Cationic, often amphiphilic, peptides with antimicrobial, antifungal, anticancer, etc., properties have been discovered in all forms of life and demonstrated a prominent role in executing the functions of life. Inspired by Nature, antimicrobial peptides (AMPs) and their synthetic analogs, with a predominantly nonspecific mode of action, are rapidly gaining attention for their clinical potential as novel antibiotics that are much less prone to drug resistance. It has recently been discovered that, beyond their antimicrobial activity inherently supporting the innate immune system, AMPs display tumor suppressive effect and influence signaling cascades that stimulate activity of the adaptive immune system. Rationally designed variations in cell penetrating peptides (CPP) have demonstrated promising potentials for drug delivery.

Numerous recent studies point to an increasing role of peptides as potential therapeutics for the treatment of a broad range of diseases. Consequently, an increasing number of peptide drug candidates that were inspired by Nature have progressed to phase clinical trials.

For this Special Issue, we invite submissions of papers focusing on understanding the challenges and opportunities for clinical development with this emerging therapeutic class.

Prof. Zofia Urbanczyk-Lipkowska
Guest Editor

Manuscript Submission Information

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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. Biomolecules 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 2700 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

  • methodology of natural peptides discovery, synthesis and characterization
  • studies on molecular mechanism of action
  • interactions with biological systems (proteins, DNA, RNA)
  • bioinspired peptides as drug delivery systems
  • clinical aspects of bioinspired peptides application

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Related Special Issue

Published Papers (10 papers)

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Research

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14 pages, 2011 KiB  
Article
Bacterial Quorum-Sensing Peptides as Immune Modulators Present in Systemic Circulation
by Anton De Spiegeleer, Amélie Descamps, Srinath Govindarajan, Julie Coudenys, Kevin Van der borght, Hannah Hirmz, Nele Van Den Noortgate, Dirk Elewaut, Bart De Spiegeleer and Evelien Wynendaele
Biomolecules 2023, 13(2), 296; https://doi.org/10.3390/biom13020296 - 4 Feb 2023
Cited by 5 | Viewed by 2750
Abstract
Quorum-sensing peptides (QSPs) are bacterial peptides traditionally considered only as inter-bacterial communication molecules. Recently, their involvement in microbiome–host interactions influencing host diseases such as cancer and sarcopenia were explored. However, it is still unknown to what extent these peptides have the potential to [...] Read more.
Quorum-sensing peptides (QSPs) are bacterial peptides traditionally considered only as inter-bacterial communication molecules. Recently, their involvement in microbiome–host interactions influencing host diseases such as cancer and sarcopenia were explored. However, it is still unknown to what extent these peptides have the potential to modulate the immune system. In this proof-of-concept study, we screened 89 QSPs for their potential to induce IL-6 and TNFα in murine splenocytes and J774 macrophages. Confirmatory experiments on the positive screening-hits were conducted using murine splenocytes and human PBMCs of different ages. Finally, to investigate the biological relevance of immunomodulatory QSPs, we analysed plasma in a human cohort for the presence of the immunomodulatory QSP Q010. To do this, we used a newly developed UHPLC-MS/MS method. Our findings indicated that specific QSPs activate immune cells in vitro, with Q007, Q010, Q017 and Q212 being the top four screening hits. Q007 and Q010 were affirmed in subsequent confirmatory experiments using murine splenocytes and human PBMCs. Finally, Q010 was detected in human plasma, demonstrating for the first time the presence of an immunomodulatory QSP in human circulation. In conclusion, our data are the first evidence indicating the potential of biologically relevant quorum-sensing peptides to modulate the immune system. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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13 pages, 3523 KiB  
Article
Dimeric Benzodiazepines as Peptide Mimetics to Overcome p53-Dependent Drug Resistance of Tumors
by Elżbieta Speina, Marcin Wilczek and Adam Mieczkowski
Biomolecules 2023, 13(2), 291; https://doi.org/10.3390/biom13020291 - 3 Feb 2023
Viewed by 1954
Abstract
Benzodiazepines that consist of one α- and one β-amino acid residues linked together in a seven-membered heterocyclic ring could be treated as small, rigid, cyclic dipeptides capable of exhibiting a wide range of biological activities. During our research on novel analogues of anthramycin, [...] Read more.
Benzodiazepines that consist of one α- and one β-amino acid residues linked together in a seven-membered heterocyclic ring could be treated as small, rigid, cyclic dipeptides capable of exhibiting a wide range of biological activities. During our research on novel analogues of anthramycin, a tricyclic antibiotic benzodiazepine, we developed the synthesis of two benzodiazepine dimers, obtained through the cyclization of appropriate linear tripeptides. The synthesized compounds were tested on a panel of seven cancer and normal cell lines. The developed molecules exhibited promising cytotoxic activity against the lung cancer cell lines A549 and NCI-H1299 and the epidermoid carcinoma cell line A-431. Moreover, they showed significant selectivity compared to the reference cell lines (BJ—human normal skin fibroblasts and MRC-5—human normal lung cell line). When tested on two isogenic cell lines, HCT116 and HCT116p53−/− (colon cancer), contrary to cisplatin being used as a positive control, the obtained compounds showed a cytotoxic effect independent of the p53 protein status. For the above reasons, the obtained compounds can be considered a new group of promising anticancer agents, useful in the fight against p53-dependent drug resistance in cancers. They can also be treated as convenient, leading structures suitable for further optimization and searching for more active and selective molecules. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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19 pages, 1597 KiB  
Article
Intact Transition Epitope Mapping—Force Differences between Original and Unusual Residues (ITEM-FOUR)
by Claudia Röwer, Christian Ortmann, Andrei Neamtu, Reham F. El-Kased and Michael O. Glocker
Biomolecules 2023, 13(1), 187; https://doi.org/10.3390/biom13010187 - 16 Jan 2023
Cited by 5 | Viewed by 2312
Abstract
Antibody-based point-of-care diagnostics have become indispensable for modern medicine. In-depth analysis of antibody recognition mechanisms is the key to tailoring the accuracy and precision of test results, which themselves are crucial for targeted and personalized therapy. A rapid and robust method is desired [...] Read more.
Antibody-based point-of-care diagnostics have become indispensable for modern medicine. In-depth analysis of antibody recognition mechanisms is the key to tailoring the accuracy and precision of test results, which themselves are crucial for targeted and personalized therapy. A rapid and robust method is desired by which binding strengths between antigens and antibodies of concern can be fine-mapped with amino acid residue resolution to examine the assumedly serious effects of single amino acid polymorphisms on insufficiencies of antibody-based detection capabilities of, e.g., life-threatening conditions such as myocardial infarction. The experimental ITEM-FOUR approach makes use of modern mass spectrometry instrumentation to investigate intact immune complexes in the gas phase. ITEM-FOUR together with molecular dynamics simulations, enables the determination of the influences of individually exchanged amino acid residues within a defined epitope on an immune complex’s binding strength. Wild-type and mutated epitope peptides were ranked according to their experimentally determined dissociation enthalpies relative to each other, thereby revealing which single amino acid polymorphism caused weakened, impaired, and even abolished antibody binding. Investigating a diagnostically relevant human cardiac Troponin I epitope for which seven nonsynonymous single nucleotide polymorphisms are known to exist in the human population tackles a medically relevant but hitherto unsolved problem of current antibody-based point-of-care diagnostics. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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15 pages, 1926 KiB  
Article
Glycosylated Lipopeptides—Synthesis and Evaluation of Antimicrobial Activity and Cytotoxicity
by Karol Sikora, Marta Bauer, Sylwia Bartoszewska, Damian Neubauer and Wojciech Kamysz
Biomolecules 2023, 13(1), 172; https://doi.org/10.3390/biom13010172 - 13 Jan 2023
Cited by 2 | Viewed by 2563
Abstract
Ultrashort cationic lipopeptides (USCLs) are promising antimicrobial agents that may be used to combat pathogens such as bacteria and fungi. USCLs consist of a few basic amino acid residues and at least one lipid moiety, usually a fatty acid chain. Generally, USCLs are [...] Read more.
Ultrashort cationic lipopeptides (USCLs) are promising antimicrobial agents that may be used to combat pathogens such as bacteria and fungi. USCLs consist of a few basic amino acid residues and at least one lipid moiety, usually a fatty acid chain. Generally, USCLs are potent antimicrobials but their major shortcoming is a relatively high cytotoxicity and hemolytic activity. Glycopeptide antibiotics (e.g. vancomycin) are essential in combating bacterial infections and are popular in medicinal practice. However, literature concerning the effect of glycosylation of peptides on their antimicrobial activity is rather scarce. For the first time, this study highlights the effect of USCLs glycosylation on in vitro biological activity. The aim of this study was to evaluate the impact of glycosylation of a series of USCLs on antimicrobial activity, cytotoxicity and hemolytic activity. Straight-chain fatty acids (C14, C16, C18) were attached to the N-terminal amino group of tripeptides—SRR-NH2, RSR-NH2 and RRS-NH2. Two groups of the lipopeptides were synthetized, the first with unmodified L-serine (USCLs) and the other with L-serine O-glycosylated by N-acetyl-β-d-glucosamine to produce new class of glycosylated ultrashort cationic lipopeptide (gUSCLs). Both USCLs and gUSCLs were tested against planktonic and biofilm cultures of ESKAPE strains (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, Enterobacter spp.) and Candida glabrata, and hemolytic activity on human erythrocytes and cytotoxicity against the HaCaT cell line was examined. Generally, USCLs and gUSCLs proved to be active against all the tested strains. The highest activity displayed was by lipopeptides containing the C18 fatty acid. Antimicrobial, hemolytic and cytotoxic activities were mainly correlated with amino acid sequence (position of serine/glycosylated serine) and hydrophobicity of molecule and were found to be highly strain-dependent. In general, glycosylation did not guarantee an increased antimicrobial activity or a decreased hemolytic and cytotoxic activities. However, in some cases, gUSCLs proved to be superior to their USCLs analogs. The most pronounced differences were found for peptides with C18 fatty acid and serine at the first and second position against both planktonic cells and biofilm of C. glabrata, as well as the second and third position against S. aureus. It is noteworthy that gUSCLs were also more active against biofilm than were USCLs. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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15 pages, 1413 KiB  
Article
Antimicrobial Spectrum of Activity and Mechanism of Action of Linear Alpha-Helical Peptides Inspired by Shrimp Anti-Lipopolysaccharide Factors
by Gabriel Machado Matos, Beatriz Garcia-Teodoro, Camila Pimentel Martins, Paulina Schmitt, Fanny Guzmán, Ana Claudia Oliveira de Freitas, Patricia Hermes Stoco, Fabienne Antunes Ferreira, Marciel João Stadnik, Diogo Robl, Luciane Maria Perazzolo and Rafael Diego Rosa
Biomolecules 2023, 13(1), 150; https://doi.org/10.3390/biom13010150 - 11 Jan 2023
Cited by 8 | Viewed by 3325
Abstract
Shrimp antilipopolysaccharide factors (ALFs) form a multifunctional and diverse family of antimicrobial host defense peptides (AMPs) composed of seven members (groups A to G), which differ in terms of their primary structure and biochemical properties. They are amphipathic peptides with two conserved cysteine [...] Read more.
Shrimp antilipopolysaccharide factors (ALFs) form a multifunctional and diverse family of antimicrobial host defense peptides (AMPs) composed of seven members (groups A to G), which differ in terms of their primary structure and biochemical properties. They are amphipathic peptides with two conserved cysteine residues stabilizing a central β-hairpin that is understood to be the core region for their biological activities. In this study, we synthetized three linear (cysteine-free) peptides based on the amino acid sequence of the central β-hairpin of the newly identified shrimp (Litopenaeus vannamei) ALFs from groups E to G. Unlike whole mature ALFs, the ALF-derived peptides exhibited an α-helix secondary structure. In vitro assays revealed that the synthetic peptides display a broad spectrum of activity against both Gram-positive and Gram-negative bacteria and fungi but not against the protozoan parasites Trypanosoma cruzi and Leishmania (L.) infantum. Remarkably, they displayed synergistic effects and showed the ability to permeabilize bacterial membranes, a mechanism of action of classical AMPs. Having shown low cytotoxicity to THP-1 human cells and being active against clinical multiresistant bacterial isolates, these nature-inspired peptides represent an interesting class of bioactive molecules with biotechnological potential for the development of novel therapeutics in medical sciences. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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19 pages, 3187 KiB  
Article
Design, Synthesis and Activity of New N1-Alkyl Tryptophan Functionalized Dendrimeric Peptides against Glioblastoma
by Marta Sowińska, Monika Szeliga, Maja Morawiak, Barbara Zabłocka and Zofia Urbanczyk-Lipkowska
Biomolecules 2022, 12(8), 1116; https://doi.org/10.3390/biom12081116 - 13 Aug 2022
Cited by 10 | Viewed by 2309
Abstract
Background: Due to resistance to conventional therapy, a blood–brain barrier that results in poor drug delivery, and a high potential for metastasis, glioblastoma (GBM) presents a great medical challenge. Since the repertoire of the possible therapies is very limited, novel therapeutic strategies require [...] Read more.
Background: Due to resistance to conventional therapy, a blood–brain barrier that results in poor drug delivery, and a high potential for metastasis, glioblastoma (GBM) presents a great medical challenge. Since the repertoire of the possible therapies is very limited, novel therapeutic strategies require new drugs as well as new approaches. The multiple roles played by L-tryptophan (Trp) in tumorigenesis of GBM and the previously found antiproliferative properties of Trp-bearing dendrimers against this malignancy prompted us to design novel polyfunctional peptide-based dendrimers covalently attached to N1-alkyl tryptophan (Trp) residues. Their antiproliferative properties against GBM and normal human astrocytes (NHA) and their antioxidant potential were tested. Methods: Two groups of amphiphilic peptide dendrimers terminated with N1-butyl and N1-aminopentane tryptophan were designed. The influence of dendrimers on viability of NHA and human GBM cell lines, displaying different genetic backgrounds and tumorigenic potentials, was determined by the MTT test. The influence of compounds on the clonogenic potential of GBM cells was assessed by colony-formation assay. Dendrimers were tested for radical scavenging potency as well as redox capability (DPPH, ABTS, and FRAP models). Results: Several peptide dendrimers functionalized with N1-alkyl-tryptophan at 5 µM concentration exhibited high selectivity towards GBM cells retaining 85–95% viable NHA cells while killing cancer cells. In both the MTT and colony-formation assays, compounds 21 (functionalized with N1-butyl-Trp and (+)8 charged) and 25 (functionalized with N1-aminopentane-Trp and (+)12 charged) showed the most promise for their development into anticancer drugs. According to ABTS, DPPH, and FRAP antioxidant tests, dendrimers functionalized with N1-alkylated Trp expressed higher ROS-scavenging capacity (ABTS and DPPH) than those with unsubstituted Trp. Conclusions: Peptide dendrimers functionalized with N1-alkyl-tryptophan showed varying toxicity to NHA, while all were toxic to GBM cells. Based on their activity towards inhibition of GBM viability and relatively mild effect on NHA cells the most advantageous were derivatives 21 and 25 with the respective di-dodecyl and dodecyl residue located at the C-terminus. As expected, peptide dendrimers functionalized with N1-alkyl-tryptophan expressed higher scavenging potency against ROS than dendrimers with unsubstituted tryptophan. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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24 pages, 8107 KiB  
Article
Peptide Dendrimers with Non-Symmetric Bola Structure Exert Long Term Effect on Glioblastoma and Neuroblastoma Cell Lines
by Marta Sowińska, Monika Szeliga, Maja Morawiak, Elżbieta Ziemińska, Barbara Zabłocka and Zofia Urbańczyk-Lipkowska
Biomolecules 2021, 11(3), 435; https://doi.org/10.3390/biom11030435 - 15 Mar 2021
Cited by 5 | Viewed by 2479
Abstract
Background: Glioblastoma (GBM) is the most common malignant tumor of the central nervous system (CNS). Neuroblastoma (NB) is one of the most common cancers of childhood derived from the neural crest cells. The survival rate for patients with GBM and high-risk NB is [...] Read more.
Background: Glioblastoma (GBM) is the most common malignant tumor of the central nervous system (CNS). Neuroblastoma (NB) is one of the most common cancers of childhood derived from the neural crest cells. The survival rate for patients with GBM and high-risk NB is poor; therefore, novel therapeutic approaches are needed. Increasing evidence suggests a dual role of redox-active compounds in both tumorigenesis and cancer treatment. Therefore, in this study, polyfunctional peptide-based dendrimeric molecules of the bola structure carrying residues with antiproliferative potential on one side and the antioxidant residues on the other side were designed. Methods: We synthesized non-symmetric bola dendrimers and assessed their radical scavenging potency as well as redox capability. The influence of dendrimers on viability of rat primary cerebellar neurons (CGC) and normal human astrocytes (NHA) was determined by propidium iodide staining and cell counting. Cytotoxicity against human GBM cell lines, T98G and LN229, and NB cell line SH-SY5Y was assessed by cell counting and colony forming assay. Results: Testing of CGC and NHA viability allowed to establish a range of optimal dendrimers structure and concentration for further evaluation of their impact on two human GBM and one human NB cell lines. According to ABTS, DPPH, FRAP, and CUPRAC antioxidant tests, the most toxic for normal cells were dendrimers with high charge and an excess of antioxidant residues (Trp and PABA) on both sides of the bola structure. At 5 μM concentration, most of the tested dendrimers neither reduced rat CGC viability below 50–40%, nor harmed human neurons (NHA). The same dose of compounds 16 or 22, after 30 min treatment decreased the number of SH-SY5Y and LN229 cells, but did not affect the number of T98G cells 48 h post treatment. However, either compound significantly reduced the number of colonies formed by SH-SY5Y, LN229, and T98G cells measured 14 days after treatment. Conclusions: Peptide dendrimers with non-symmetric bola structure are excellent scaffolds for design of molecules with pro/antioxidant functionality. Design of molecules with an excess of positive charges and antioxidant residues rendered molecules with high neurotoxicity. Single, 30 min exposition of the GBM and NB cell lines to the selected bola dendrimers significantly suppressed their clonogenic potential Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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Review

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27 pages, 2553 KiB  
Review
Antimicrobial Peptides (AMPs): Potential Therapeutic Strategy against Trypanosomiases?
by Maura Rojas-Pirela, Ulrike Kemmerling, Wilfredo Quiñones, Paul A. M. Michels and Verónica Rojas
Biomolecules 2023, 13(4), 599; https://doi.org/10.3390/biom13040599 - 26 Mar 2023
Cited by 7 | Viewed by 4213
Abstract
Trypanosomiases are a group of tropical diseases that have devastating health and socio-economic effects worldwide. In humans, these diseases are caused by the pathogenic kinetoplastids Trypanosoma brucei, causing African trypanosomiasis or sleeping sickness, and Trypanosoma cruzi, causing American trypanosomiasis or Chagas [...] Read more.
Trypanosomiases are a group of tropical diseases that have devastating health and socio-economic effects worldwide. In humans, these diseases are caused by the pathogenic kinetoplastids Trypanosoma brucei, causing African trypanosomiasis or sleeping sickness, and Trypanosoma cruzi, causing American trypanosomiasis or Chagas disease. Currently, these diseases lack effective treatment. This is attributed to the high toxicity and limited trypanocidal activity of registered drugs, as well as resistance development and difficulties in their administration. All this has prompted the search for new compounds that can serve as the basis for the development of treatment of these diseases. Antimicrobial peptides (AMPs) are small peptides synthesized by both prokaryotes and (unicellular and multicellular) eukaryotes, where they fulfill functions related to competition strategy with other organisms and immune defense. These AMPs can bind and induce perturbation in cell membranes, leading to permeation of molecules, alteration of morphology, disruption of cellular homeostasis, and activation of cell death. These peptides have activity against various pathogenic microorganisms, including parasitic protists. Therefore, they are being considered for new therapeutic strategies to treat some parasitic diseases. In this review, we analyze AMPs as therapeutic alternatives for the treatment of trypanosomiases, emphasizing their possible application as possible candidates for the development of future natural anti-trypanosome drugs. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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15 pages, 511 KiB  
Review
Polymorphisms in Genes Involved in Inflammation and Periodontitis: A Narrative Review
by Aniela Brodzikowska and Bartłomiej Górski
Biomolecules 2022, 12(4), 552; https://doi.org/10.3390/biom12040552 - 7 Apr 2022
Cited by 17 | Viewed by 3181
Abstract
Current evidence pinpoints that the variability in periodontitis traits in humans may be attributable to genetic factors. Different allelic variants can result in alterations in tissue structure, antibody responses and inflammatory mediators. Consequently, genetic variations may act as protective or risk factors for [...] Read more.
Current evidence pinpoints that the variability in periodontitis traits in humans may be attributable to genetic factors. Different allelic variants can result in alterations in tissue structure, antibody responses and inflammatory mediators. Consequently, genetic variations may act as protective or risk factors for periodontal diseases. A number of features of the inflammatory and immune response that seem to play a role in the development of periodontitis have a clearly established genetic basis. Identifying genes that contribute to the pathogenesis of periodontitis may be utilized for risk assessment in both aggressive and chronic periodontitis. The aim of this narrative review is to summarize the role of polymorphisms in genes involved in inflammation and periodontitis, including cellular receptors, tissue compatibility antigens, antibodies and cytokines. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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17 pages, 612 KiB  
Review
Histatin 5 Metallopeptides and Their Potential against Candida albicans Pathogenicity and Drug Resistance
by Gabriela Vieira Silva Zolin, Fauller Henrique da Fonseca, Carolina Reis Zambom and Saulo Santesso Garrido
Biomolecules 2021, 11(8), 1209; https://doi.org/10.3390/biom11081209 - 13 Aug 2021
Cited by 15 | Viewed by 4286
Abstract
Usually caused by Candida albicans, buccal candidiasis begins with the morphological transition between yeast and hyphal cells. Over time and without the correct treatment, it can be disseminated through the bloodstream becoming a systemic infection with high mortality rates. C. albicans [...] Read more.
Usually caused by Candida albicans, buccal candidiasis begins with the morphological transition between yeast and hyphal cells. Over time and without the correct treatment, it can be disseminated through the bloodstream becoming a systemic infection with high mortality rates. C. albicans already shows resistance against antifungals commonly used in treatments. Therefore, the search for new drugs capable of overcoming antifungal resistance is essential. Histatin 5 (Hst5) is an antimicrobial peptide of the Histatin family, that can be found naturally in human saliva. This peptide presents high antifungal activity against C. albicans. However, Hst5 action can be decreased for interaction with enzymes and metal ions present in the oral cavity. The current work aims to bring a brief review of relevant aspects of the pathogenesis and resistance mechanisms already reported for C. albicans. In addition, are also reported here the main immune responses of the human body and the most common antifungal drugs. Finally, the most important aspects regarding Histatin 5 and the benefits of its interaction with metals are highlighted. The intention of this review is to show the promising use of Hst5 metallopeptides in the development of effective drugs. Full article
(This article belongs to the Special Issue Nature Inspired Peptides in Medical Sciences)
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