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Membranes
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Modern Studies on Membrane-Targeting Antimicrobial Peptides
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Modern Studies on Membrane-Targeting Antimicrobial Peptides

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membrane Functions".

Deadline for manuscript submissions: closed (25 May 2023) | Viewed by 15212

Special Issue Editors

Dr. Ekaterina I. Finkina

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Guest Editor
M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia
Interests: plant innate immunity; plant pathogenesis related proteins (PR-proteins); lipid transfer proteins (LTPs); defensins; Bet v 1 homologues; lipid binding; antimicrobial activity; membrane permeability; recombinant expression of proteins; plant allergens; allergy; sensitization
Special Issues, Collections and Topics in MDPI journals
Dr. Sergey V. Balandin

E-Mail Website
Guest Editor
Russian Academy of Sciences, Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, 117997 Moscow, Russia
Interests: antibiotics; antimicrobial peptides; bacteriocins; lantibiotics; pediocin-like peptides; molecular evolution; protein expression and purification; synthetic biology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Over the past decades, thousands of natural antimicrobial peptides (AMPs) have been isolated from representatives of all kingdoms of life. Most of them are genetically encoded products of ribosomal synthesis that undergo minor post-translational modifications. Thanks to the development of NGS technologies, a huge number of potentially active homologous structures have been identified in the sequenced genomes and transcriptomes of many prokaryotic and eukaryotic species. In multicellular organisms, AMPs are effectors and regulators of innate immunity, while in unicellular organisms they play the role of signaling and aggression instruments in the struggle for an ecological niche. The direct antimicrobial action of AMP in most cases is due to their membrane-targeting mechanism of action, which can optionally involve interaction with a specific membrane component or receptor and, ultimately, ends with the incorporation of the peptide into the lipid bilayer and disruption of the membrane barrier function. Some AMPs use their membrane activity to penetrate into the cytoplasm of the target cell where they interfere with such processes as transcription or translation. AMPs are considered as prototypes of a new generation of antibacterial and antifungal agents active against pathogenic strains resistant to conventional antibiotics. The COVID-19 pandemic has further updated research in this field since superinfections (including multidrug-resistant acquired during hospitalization) are a factor that aggravates the course of the disease and increases mortality.

This Special Issue is aimed at demonstrating recent advances in the study of the structure and functional activity of natural and artificial membrane-targeting AMPs, the study of physicochemical and biological aspects of their mechanism of action, including interaction with lipid or protein components of target cell membranes. The data obtained on living cells and simplified model systems, such as micelles or liposomes, may be presented, which may be supported by in silico simulations. Both experimental articles and reviews are welcome.

Kind regards,
Dr. Ekaterina I. Finkina
Dr. Sergey V. Balandin
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. Membranes 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 2200 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 peptide (AMP)
  • structure and functional activity
  • membrane-targeting mechanism of action
  • membrane permeability
  • interaction with lipid or protein components of target cell membranes

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Published Papers (6 papers)

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Research

15 pages, 3246 KiB  
Article
Genomic Insights into Bacterial Resistance to Proline-Rich Antimicrobial Peptide Bac7
by Pavel V. Panteleev, Victoria N. Safronova, Roman N. Kruglikov, Ilia A. Bolosov and Tatiana V. Ovchinnikova
Membranes 2023, 13(4), 438; https://doi.org/10.3390/membranes13040438 - 17 Apr 2023
Cited by 1 | Viewed by 2024
Abstract
Proline-rich antimicrobial peptides (PrAMPs) having a potent antimicrobial activity and a modest toxicity toward mammalian cells attract much attention as new templates for the development of antibiotic drugs. However, a comprehensive understanding of mechanisms of bacterial resistance development to PrAMPs is necessary before [...] Read more.
Proline-rich antimicrobial peptides (PrAMPs) having a potent antimicrobial activity and a modest toxicity toward mammalian cells attract much attention as new templates for the development of antibiotic drugs. However, a comprehensive understanding of mechanisms of bacterial resistance development to PrAMPs is necessary before their clinical application. In this study, development of the resistance to the proline-rich bovine cathelicidin Bac71-22 derivative was characterized in the multidrug-resistant Escherichia coli clinical isolate causing the urinary tract infection. Three Bac71-22-resistant strains with ≥16-fold increase in minimal inhibitory concentrations (MICs) were selected by serially passaging after four-week experimental evolution. It was shown that in salt-containing medium, the resistance was mediated by inactivation of the SbmA transporter. The absence of salt in the selection media affected both dynamics and main molecular targets under selective pressure: a point mutation leading to the amino acid substitution N159H in the WaaP kinase responsible for heptose I phosphorylation in the LPS structure was also found. This mutation led to a phenotype with a decreased susceptibility to both the Bac71-22 and polymyxin B. Screening of antimicrobial activities with the use of a wide panel of known AMPs, including the human cathelicidin LL-37 and conventional antibiotics, against selected strains indicated no significant cross-resistance effects. Full article
(This article belongs to the Special Issue Modern Studies on Membrane-Targeting Antimicrobial Peptides)
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14 pages, 7680 KiB  
Article
γ-Core Guided Antibiotic Design Based on Human Enteric Defensin 5
by Gaomei Zhao, Changsheng Jia, Cheng Zhu, Minchao Fang, Chenwenya Li, Yin Chen, Yingjuan He, Songling Han, Yongwu He, Jining Gao, Tao Wang, Cheng Wang and Junping Wang
Membranes 2023, 13(1), 51; https://doi.org/10.3390/membranes13010051 - 31 Dec 2022
Cited by 1 | Viewed by 2199
Abstract
An increase in the number of infections caused by resistant bacteria worldwide necessitates the development of alternatives to antibiotics. Human defensin (HD) 5 is an innate immune peptide with broad-spectrum antibacterial activity, but its complicated structure makes its preparation difficult. Herein, we truncated [...] Read more.
An increase in the number of infections caused by resistant bacteria worldwide necessitates the development of alternatives to antibiotics. Human defensin (HD) 5 is an innate immune peptide with broad-spectrum antibacterial activity, but its complicated structure makes its preparation difficult. Herein, we truncated the HD5 structure by extracting the highly conserved γ-core motif. A structure-activity study showed that this motif was ineffective in killing bacteria in the absence of specific spatial conformation. Notably, after the introduction of two intramolecular disulfide bonds, its antibacterial activity was markedly improved. Glu and Ser residues were then replaced with Arg to create the derivative RC18, which exhibited stronger potency than HD5, particularly against methicillin-resistant S. aureus (MRSA). Mechanistically, RC18 bound to lipid A and lipoteichoic acid at higher affinities than HD5. Furthermore, RC18 was more efficient than HD5 in penetrating the bacterial membranes. Molecular dynamics simulation revealed that five Arg residues, Arg1, Arg7, Arg9, Arg15, and Arg18, mediated most of the polar interactions of RC18 with the phospholipid head groups during membrane penetration. In vivo experiments indicated that RC18 decreased MRSA colonization and dramatically improved the survival of infected mice, thus demonstrating that RC18 is a promising drug candidate to treat MRSA infections. Full article
(This article belongs to the Special Issue Modern Studies on Membrane-Targeting Antimicrobial Peptides)
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19 pages, 2468 KiB  
Article
Antimicrobial Activity and Immunomodulatory Properties of Acidocin A, the Pediocin-like Bacteriocin with the Non-Canonical Structure
by Daria V. Antoshina, Sergey V. Balandin, Ivan V. Bogdanov, Maria A. Vershinina, Elvira V. Sheremeteva, Ilia Yu. Toropygin, Ekaterina I. Finkina and Tatiana V. Ovchinnikova
Membranes 2022, 12(12), 1253; https://doi.org/10.3390/membranes12121253 - 11 Dec 2022
Cited by 10 | Viewed by 2509
Abstract
Pediocin-like bacteriocins are among the natural antimicrobial agents attracting attention as scaffolds for the development of a new generation of antibiotics. Acidocin A has significant structural differences from most other members of this subclass. We studied its antibacterial and cytotoxic activity, as well [...] Read more.
Pediocin-like bacteriocins are among the natural antimicrobial agents attracting attention as scaffolds for the development of a new generation of antibiotics. Acidocin A has significant structural differences from most other members of this subclass. We studied its antibacterial and cytotoxic activity, as well as effects on the permeability of E. coli membranes in comparison with avicin A, the typical pediocin-like bacteriocin. Acidocin A had a more marked tendency to form an alpha-helical structure upon contact with detergent micelles, as was shown by CD spectroscopy, and demonstrated considerably less specific mode of action: it inhibited growth of Gram-positive and Gram-negative strains, which were unsusceptible to avicin A, and disrupted the integrity of outer and inner membranes of E. coli. However, the peptide retained a low toxicity towards normal and tumor human cells. The effect of mutations in the pediocin box of acidocin A (on average, a 2–4-fold decrease in activity) was less pronounced than is usually observed for such peptides. Using multiplex analysis, we showed that acidocin A and avicin A modulated the expression level of a number of cytokines and growth factors in primary human monocytes. Acidocin A induced the production of a number of inflammatory mediators (IL-6, TNFα, MIG/CXCL9, MCP-1/CCL2, MCP-3/CCL7, and MIP-1β) and inhibited the production of some anti-inflammatory factors (IL-1RA, MDC/CCL22). We assumed that the activity of acidocin A and similar peptides produced by lactic acid bacteria might affect the functional state of the human intestinal tract, not only through direct inhibition of various groups of symbiotic and pathogenic bacteria, but also via immunomodulatory effects. Full article
(This article belongs to the Special Issue Modern Studies on Membrane-Targeting Antimicrobial Peptides)
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14 pages, 3516 KiB  
Article
Arginine Homopeptide of 11 Residues as a Model of Cell-Penetrating Peptides in the Interaction with Bacterial Membranes
by Mónica Aróstica, Roberto Rojas, Luis Felipe Aguilar, Patricio Carvajal-Rondanelli, Fernando Albericio, Fanny Guzmán and Constanza Cárdenas
Membranes 2022, 12(12), 1180; https://doi.org/10.3390/membranes12121180 - 24 Nov 2022
Cited by 3 | Viewed by 2037
Abstract
Cell-penetrating peptides rich in arginine are good candidates to be considered as antibacterial compounds, since peptides have a lower chance of generating resistance than commonly used antibiotics. Model homopeptides are a useful tool in the study of activity and its correlation with a [...] Read more.
Cell-penetrating peptides rich in arginine are good candidates to be considered as antibacterial compounds, since peptides have a lower chance of generating resistance than commonly used antibiotics. Model homopeptides are a useful tool in the study of activity and its correlation with a secondary structure, constituting an initial step in the construction of functional heteropeptides. In this report, the 11-residue arginine homopeptide (R11) was used to determine its antimicrobial activity against Staphylococcus aureus and Escherichia coli and the effect on the secondary structure, caused by the substitution of the arginine residue by the amino acids Ala, Pro, Leu and Trp, using the scanning technique. As a result, most of the substitutions improved the antibacterial activity, and nine peptides were significantly more active than R11 against the two tested bacteria. The cell-penetrating characteristic of the peptides was verified by SYTOX green assay, with no disruption to the bacterial membranes. Regarding the secondary structure in four different media—PBS, TFE, E. coli membrane extracts and DMPG vesicles—the polyproline II structure, the one of the parent R11, was not altered by unique substitutions, although the secondary structure of the peptides was best defined in E. coli membrane extract. This work aimed to shed light on the behavior of the interaction model of penetrating peptides and bacterial membranes to enhance the development of functional heteropeptides. Full article
(This article belongs to the Special Issue Modern Studies on Membrane-Targeting Antimicrobial Peptides)
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17 pages, 3495 KiB  
Article
Antifungal Activity, Structural Stability, and Immunomodulatory Effects on Human Immune Cells of Defensin from the Lentil Lens culinaris
by Ekaterina I. Finkina, Ivan V. Bogdanov, Anastasia A. Ignatova, Marina D. Kanushkina, Ekaterina A. Egorova, Alexander D. Voropaev, Elena A. Stukacheva and Tatiana V. Ovchinnikova
Membranes 2022, 12(9), 855; https://doi.org/10.3390/membranes12090855 - 31 Aug 2022
Cited by 7 | Viewed by 2227
Abstract
An increase in the frequency of mycoses and spreading of multidrug-resistant fungal pathogens necessitates the search for new antifungal agents. Earlier, we isolated the novel defensin from lentil Lensculinaris seeds, designated as Lc-def, which inhibited the growth of phytopathogenic fungi. Here, we [...] Read more.
An increase in the frequency of mycoses and spreading of multidrug-resistant fungal pathogens necessitates the search for new antifungal agents. Earlier, we isolated the novel defensin from lentil Lensculinaris seeds, designated as Lc-def, which inhibited the growth of phytopathogenic fungi. Here, we studied an antifungal activity of Lc-def against human pathogenic Candida species, structural stability of the defensin, and its immunomodulatory effects that may help to prevent fungal infection. We showed that Lc-def caused 50% growth inhibition of clinical isolates of Candida albicans, C. krusei, and C. glabrata at concentrations of 25–50 μM, but was not toxic to different human cells. The lentil defensin was resistant to proteolysis by C. albicans and was not cleaved during simulated gastroduodenal digestion. By using the multiplex xMAP assay, we showed for the first time for plant defensins that Lc-def increased the production of such essential for immunity to candidiasis pro-inflammatory cytokines as IL-12 and IL-17 at the concentration of 2 μM. Thus, we hypothesized that the lentil Lc-def and plant defensins in general may be effective in suppressing of mucocutaneous candidiasis due to their antifungal activity, high structural stability, and ability to activate a protective immune response. Full article
(This article belongs to the Special Issue Modern Studies on Membrane-Targeting Antimicrobial Peptides)
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18 pages, 5252 KiB  
Article
A Novel Proline-Rich Cathelicidin from the Alpaca Vicugna pacos with Potency to Combat Antibiotic-Resistant Bacteria: Mechanism of Action and the Functional Role of the C-Terminal Region
by Pavel V. Panteleev, Victoria N. Safronova, Roman N. Kruglikov, Ilia A. Bolosov, Ivan V. Bogdanov and Tatiana V. Ovchinnikova
Membranes 2022, 12(5), 515; https://doi.org/10.3390/membranes12050515 - 12 May 2022
Cited by 9 | Viewed by 3130
Abstract
Over recent years, a growing number of bacterial species have become resistant to clinically relevant antibiotics. Proline-rich antimicrobial peptides (PrAMPs) having a potent antimicrobial activity and a negligible toxicity toward mammalian cells attract attention as new templates for the development of antibiotic drugs. [...] Read more.
Over recent years, a growing number of bacterial species have become resistant to clinically relevant antibiotics. Proline-rich antimicrobial peptides (PrAMPs) having a potent antimicrobial activity and a negligible toxicity toward mammalian cells attract attention as new templates for the development of antibiotic drugs. Here, we mined genomes of all living Camelidae species and found a novel family of Bac7-like proline-rich cathelicidins which inhibited bacterial protein synthesis. The N-terminal region of a novel peptide from the alpaca Vicugna pacos named VicBac is responsible for inhibition of bacterial protein synthesis with an IC50 value of 0.5 µM in the E. coli cell-free system whereas the C-terminal region allows the peptide to penetrate bacterial membranes effectively. We also found that the full-length VicBac did not induce bacterial resistance after a two-week selection experiment, unlike the N-terminal truncated analog, which depended on the SbmA transport system. Both pro- and anti-inflammatory action of VicBac and its N-terminal truncated variant on various human cell types was found by multiplex immunoassay. The presence of the C-terminal tail in the natural VicBac does not provide for specific immune-modulatory effects in vitro but enhances the observed impact compared with the truncated analog. The pronounced antibacterial activity of VicBac, along with its moderate adverse effects on mammalian cells, make this molecule a promising scaffold for the development of peptide antibiotics. Full article
(This article belongs to the Special Issue Modern Studies on Membrane-Targeting Antimicrobial Peptides)
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