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Antimicrobial Peptides 2022
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Antimicrobial Peptides 2022

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Medicinal Chemistry".

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 14613

Special Issue Editor

Dr. Eugene A. Rogozhin

E-Mail Website
Guest Editor
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, RAS, Moscow, Russia
Interests: plant antimicrobial peptides; peptide antibiotic; medicinal plants; defense peptides; plant innate immunity

Special Issue Information

Dear Colleagues,

Antimicrobial peptides (AMPs) are known to present “a first defense line” of many organisms against pathogens, which are a driving force of biotic stress. As a rule, AMPs are the components of innate immune systems, which is why they are typical for their wide structural diversity and mode of action determining their specificity. We welcome you to prepare and submit manuscripts describing absolutely novel or homologous antimicrobial peptides isolated from bacteria, fungi, plants and invertebrates: structure determination, 3D modeling, rational design and studying of mechanisms of interaction with target microbes (pathogenic bacteria, yeasts and filamentous fungi) at cellular and molecular levels are invited to be presented. Additionally, AMPs from natural sources can be presented as potential antifungal (fungicidal or fungistatic) and antitumor compounds based on their cytotoxity, inhibition of key enzymes, suppression of transcription of some target genes, DNA-binding etc. A key focus of the Special Issue is the presentation of natural AMPs with alternative modes of action that realize at different active concentrations, for example.

We hope that novel data about structure-function relationships among natural AMPs will allow making a contribution to our knowledge in this scientific direction.

Dr. Eugene Rogozhin
Guest Editor

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. Molecules is an international peer-reviewed open access semimonthly 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

  • antimicrobial peptides
  • natural sources
  • structure elicitation
  • molecular modeling
  • antifungal activity
  • antitumor activity
  • mode of action
  • membrane-active peptides

Published Papers (5 papers)

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Research

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17 pages, 8483 KiB  
Article
Antitumor Activity and Mechanism of Action of the Antimicrobial Peptide AMP-17 on Human Leukemia K562 Cells
by Zhuqing Tian, Longbing Yang, Mingjiao Huang, Chaoqin Sun, Mingming Chen, Wenjing Zhao, Jian Peng and Guo Guo
Molecules 2022, 27(22), 8109; https://doi.org/10.3390/molecules27228109 - 21 Nov 2022
Cited by 3 | Viewed by 1720
Abstract
Cancer is one of the most common malignant diseases in the world. Hence, there is an urgent need to search for novel drugs with antitumor activity against cancer cells. AMP-17, a natural antimicrobial peptide derived from Musca domestica, has antimicrobial activity against [...] Read more.
Cancer is one of the most common malignant diseases in the world. Hence, there is an urgent need to search for novel drugs with antitumor activity against cancer cells. AMP-17, a natural antimicrobial peptide derived from Musca domestica, has antimicrobial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. However, its antitumor activity and potential mechanism of action in cancer cells remain unclear. In this study, we focused on evaluating the in vitro antitumor activity and mechanism of AMP-17 on leukemic K562 cells. The results showed that AMP-17 exhibited anti-proliferative activity on K562 cells with an IC50 value of 58.91 ± 3.57 μg/mL. The membrane integrity of K562 was disrupted and membrane permeability was increased after AMP-17 action. Further observation using SEM and TEM images showed that the cell structure of AMP-17-treated cells was disrupted, with depressions and pore-like breaks on the cell surface, and vacuolated vesicles in the cytoplasm. Furthermore, further mechanistic studies indicated that AMP-17 induced excessive production of reactive oxygen species and calcium ions release in K562 cells, which led to disturbance of mitochondrial membrane potential and blocked ATP synthesis, followed by activation of Caspase-3 to induce apoptosis. In conclusion, these results suggest that the antitumor activity of AMP-17 may be achieved by disrupting cell structure and inducing apoptosis. Therefore, AMP-17 is expected to be a novel potential agent candidate for leukemia treatment. Full article
(This article belongs to the Special Issue Antimicrobial Peptides 2022)
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10 pages, 984 KiB  
Article
Rational Design of Plant Hairpin-like Peptide EcAMP1: Structural–Functional Correlations to Reveal Antibacterial and Antifungal Activity
by Anna S. Barashkova, Dmitry Y. Ryazantsev and Eugene A. Rogozhin
Molecules 2022, 27(11), 3554; https://doi.org/10.3390/molecules27113554 - 31 May 2022
Cited by 3 | Viewed by 1515
Abstract
Plant antimicrobial peptides from the α-hairpinins family (hairpin-like peptides) are known to possess a wide range of biological activities. However, less is known about the structural determinants of their antimicrobial activity. Here, we suggest that spatial structure as well as surface charge and [...] Read more.
Plant antimicrobial peptides from the α-hairpinins family (hairpin-like peptides) are known to possess a wide range of biological activities. However, less is known about the structural determinants of their antimicrobial activity. Here, we suggest that spatial structure as well as surface charge and hydrophobicity level contribute to the antimicrobial properties of α-hairpinin EcAMP1 from barnyard grass (Echinochloa cruss-galli) seeds. To examine the role of the peptide spatial structure, two truncated forms of EcAMP1 restricted by inner and outer cysteine pairs were synthesized. It was shown that both truncated forms of EcAMP1 lost their antibacterial activity. In addition, their antifungal activity became weaker. To review the contribution of surface charge and hydrophobicity, another two peptides were designed. One of them carried single amino acid substitution from tryptophan to alanine residue at the 20th position. The second one represented a truncated form of the native EcAMP1 lacking six C-terminal residues. But the α-helix was kept intact. It was shown that the antifungal activity of both modified peptides weakened. Thereby we can conclude that the secondary structural integrity, hydrophobic properties, and surface charge all play roles in the antimicrobial properties of α-hairpinins. In addition, the antibacterial activity of cereal α-hairpinins against Gram-positive bacteria was described for the first time. This study expands on the knowledge of structure–function interactions in antimicrobial α-hairpinins. Full article
(This article belongs to the Special Issue Antimicrobial Peptides 2022)
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16 pages, 1309 KiB  
Article
Immunomodulatory Responses of Two Synthetic Peptides against Salmonella Typhimurium Infection
by Marco Antonio Ibarra-Valencia, Gerardo Pável Espino-Solis, Blanca Elisa Estrada and Gerardo Corzo
Molecules 2021, 26(18), 5573; https://doi.org/10.3390/molecules26185573 - 14 Sep 2021
Cited by 2 | Viewed by 2430
Abstract
In vitro assays of phagocytic activity showed that the peptide Pin2[G] stimulates phagocytosis in BMDM cells from 0.15 to 1.25 μg/mL, and in RAW 264.7 cells at 0.31 μg/mL. In the same way, the peptide FA1 induced phagocytosis in BMDM cells from 1.17 [...] Read more.
In vitro assays of phagocytic activity showed that the peptide Pin2[G] stimulates phagocytosis in BMDM cells from 0.15 to 1.25 μg/mL, and in RAW 264.7 cells at 0.31 μg/mL. In the same way, the peptide FA1 induced phagocytosis in BMDM cells from 1.17 to 4.69 μg/mL and in RAW 264.7 cells at 150 μg/mL. Cytokine profiles of uninfected RAW 264.7 showed that Pin2[G] increased liberation TNF (from 1.25 to 10 μg/mL) and MCP-1 (10 μg/mL), and FA1 also increased the release of TNF (from 18.75 to 75 μg/mL) but did not increase the liberation of MCP-1. In RAW 264.7 macrophages infected with Salmonella enterica serovar Typhimurium, the expression of TNF increases with Pin2[G] (1.25–10 μg/mL) or FA1 (18.75–75 μg/mL). In these cells, FA1 also increases the expression of IL-12p70, IL-10 and IFN-γ when applied at concentrations of 37.5, 75 and 150 μg/mL, respectively. On the other hand, stimulation with 1.25 and 10 μg/mL of Pin2[G] promotes the expression of MCP-1 and IL-12p70, respectively. Finally, peptides treatment did not resolve murine gastric infection, but improves their physical condition. Cytokine profiles showed that FA1 reduces IFN-γ and MCP-1 but increases IL-10, while Pin2[G] reduces IFN-γ but increases the liberation of IL-6 and IL-12p70. This data suggests a promising activity of FA1 and Pin2[G] as immunomodulators of gastric infections in S. Typhimurium. Full article
(This article belongs to the Special Issue Antimicrobial Peptides 2022)
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Review

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16 pages, 2546 KiB  
Review
Marine Antimicrobial Peptides-Based Strategies for Tackling Bacterial Biofilm and Biofouling Challenges
by Anupam Patra, Jhilik Das, Nupur Rani Agrawal, Gajraj Singh Kushwaha, Mrinmoy Ghosh and Young-Ok Son
Molecules 2022, 27(21), 7546; https://doi.org/10.3390/molecules27217546 - 03 Nov 2022
Cited by 9 | Viewed by 2479
Abstract
An assemblage nexus of microorganisms enclosed in a composite extracellular polymeric matrix is called as a biofilm. The main factor causing biological fouling, or biofouling, is biofilms. Biofilm-mediated biofouling is a significant detrimental issue in several industries, including the maritime environment, industrial facilities, [...] Read more.
An assemblage nexus of microorganisms enclosed in a composite extracellular polymeric matrix is called as a biofilm. The main factor causing biological fouling, or biofouling, is biofilms. Biofilm-mediated biofouling is a significant detrimental issue in several industries, including the maritime environment, industrial facilities, water treatment facilities, and medical implants. Conventional antibacterial remedies cannot wholly eradicate bacterial species owing to the structural rigidity of biofilm and the eventual growth of antibiotic-resistant microorganisms. Consequently, several approaches to disrupt the biofilm have been investigated to address this particular phenomenon. Antimicrobial peptides (AMPs) have emerged as a promising contender in this category, offering several advantages over traditional solutions, including broad-spectrum action and lack of antibiotic resistance. Because biofouling significantly impacts the marine industry, AMPs derived from marine sources may be suitable natural inhibitors of bacterial proliferation. In this article, we discuss the range of physicochemical and structural diversity and the model of action seen in marine AMPs. This makes them an appealing strategy to mitigate biofilm and biofilm-mediated biofouling. This review also systematically summarizes recent research on marine AMPs from vertebrates and invertebrates and their industrial significance, shedding light on developing even better anti-biofouling materials shortly. Full article
(This article belongs to the Special Issue Antimicrobial Peptides 2022)
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18 pages, 848 KiB  
Review
Activity and Mechanism of Action of Antifungal Peptides from Microorganisms: A Review
by Tianxi Li, Lulu Li, Fangyuan Du, Lei Sun, Jichao Shi, Miao Long and Zeliang Chen
Molecules 2021, 26(11), 3438; https://doi.org/10.3390/molecules26113438 - 05 Jun 2021
Cited by 47 | Viewed by 5202
Abstract
Harmful fungi in nature not only cause diseases in plants, but also fungal infection and poisoning when people and animals eat food derived from crops contaminated with them. Unfortunately, such fungi are becoming increasingly more resistant to traditional synthetic antifungal drugs, which can [...] Read more.
Harmful fungi in nature not only cause diseases in plants, but also fungal infection and poisoning when people and animals eat food derived from crops contaminated with them. Unfortunately, such fungi are becoming increasingly more resistant to traditional synthetic antifungal drugs, which can make prevention and control work increasingly more difficult to achieve. This means they are potentially very harmful to human health and lifestyle. Antifungal peptides are natural substances produced by organisms to defend themselves against harmful fungi. As a result, they have become an important research object to help deal with harmful fungi and overcome their drug resistance. Moreover, they are expected to be developed into new therapeutic drugs against drug-resistant fungi in clinical application. This review focuses on antifungal peptides that have been isolated from bacteria, fungi, and other microorganisms to date. Their antifungal activity and factors affecting it are outlined in terms of their antibacterial spectra and effects. The toxic effects of the antifungal peptides and their common solutions are mentioned. The mechanisms of action of the antifungal peptides are described according to their action pathways. The work provides a useful reference for further clinical research and the development of safe antifungal drugs that have high efficiencies and broad application spectra. Full article
(This article belongs to the Special Issue Antimicrobial Peptides 2022)
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