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Creation of New Antimicrobial Peptides 3.0
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Creation of New Antimicrobial Peptides 3.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: closed (28 February 2024) | Viewed by 10608

Special Issue Editor

Prof. Dr. Oxana V. Galzitskaya

E-Mail Website
Guest Editor
1. Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia
2. Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia
Interests: protein folding; bioinformatics and proteomics; aggregation; Alzheimer’s disease; intrinsically disordered proteins; antibacterial peptides
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

World Health Organization (WHO) classifies polyresistant bacteria as a serious health hazard. In the last ten years, bacteria resistant to multiple drug dependences are have become a serious challenge for prophylactics and the treatment of many bacterial diseases. Available antibiotics are gradually becoming ineffective as a result of the resistance of bacterial cells, so it is necessary to find new antibacterial strategies to combat pathogenic organisms. Most new antibiotics are variants or combinations of existing therapeutic drugs. The world is faced with the problem of developing new strategies and technologies for combating pathogenic bacteria (bacterial diseases), and, on their basis, is creating new-generation antibacterial drugs. Around 12–17 microorganisms cause 80%–87% of nosocomial infections. Among them are S. aureus and P. aeruginosa. Among these pathogens, 16%–20% include multidrug-resistant phenotypes.

Antimicrobial peptides are diverse in terms of structure and mode of action, display broad-spectrum antimicrobial activity, and thus show promise for engineering pathogen resistance and development of novel pharmaceuticals. Novel antimicrobial peptides are under development. The creation of a novel technology and new antibiotics based on it will be a breakthrough in this field of research. The most decisive advantage of antibacterial peptides is the following: (1) the possibility to construct peptides of directional effect and (2) biological compatibility due to their natural origin.

In this Special Issue, the authors present new antimicrobial peptides and a new strategy for combating pathogenic microbes.

Prof. Dr. Oxana V. Galzitskaya
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • anti-infective agents
  • antimicrobial peptide
  • bacterial infection
  • induced resistance

Published Papers (5 papers)

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Research

19 pages, 2389 KiB  
Article
Polymyxin B Conjugates with Bio-Inspired Synthetic Polymers of Different Nature
by Anna Dvoretckaia, Tatiana Egorova, Apollinariia Dzhuzha, Mariia Levit, Eugene Sivtsov, Elena Demyanova and Evgenia Korzhikova-Vlakh
Int. J. Mol. Sci. 2023, 24(3), 1832; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms24031832 - 17 Jan 2023
Cited by 6 | Viewed by 1739
Abstract
The emergence and growth of bacterial resistance to antibiotics poses an enormous threat to humanity in the future. In this regard, the discovery of new antibiotics and the improvement of existing ones is a priority task. In this study, we proposed the synthesis [...] Read more.
The emergence and growth of bacterial resistance to antibiotics poses an enormous threat to humanity in the future. In this regard, the discovery of new antibiotics and the improvement of existing ones is a priority task. In this study, we proposed the synthesis of new polymeric conjugates of polymyxin B, which is a clinically approved but limited-use peptide antibiotic. In particular, three carboxylate-bearing polymers and one synthetic glycopolymer were selected for conjugation with polymyxin B (PMX B), namely, poly(α,L-glutamic acid) (PGlu), copolymer of L-glutamic acid and L-phenylalanine (P(Glu-co-Phe)), copolymer of N-vinyl succinamic acid and N-vinylsuccinimide (P(VSAA-co-VSI)), and poly(2-deoxy-2-methacrylamido-D-glucose) (PMAG). Unlike PGlu and PMAG, P(Glu-co-Phe) and P(VSAA-co-VSI) are amphiphilic and form nanoparticles in aqueous media. A number of conjugates with different polymyxin B loading were synthesized and characterized. In addition, the complex conjugates of PGLu or PMAG with polymyxin B and deferoxamine (siderophore) were obtained. A release of PMX B from Schiff base and amide-linked polymer conjugates was studied in model buffer media with pH 7.4 and 5.8. In both cases, a more pronounced release was observed under slightly acidic conditions. The cytotoxicity of free polymers and PMX B as well as their conjugates was examined in human embryonic kidney cells (HEK 293T cell line). All conjugates demonstrated reduced cytotoxicity compared to the free antibiotic. Finally, the antimicrobial efficacy of the conjugates against Pseudomonas aeruginosa was determined and compared. The lowest values of minimum inhibitory concentrations (MIC) were observed for polymyxin B and polymyxin B/deferoxamine conjugated with PMAG. Among the polymers tested, PMAG appears to be the most promising carrier for delivery of PMX B in conjugated form due to the good preservation of the antimicrobial properties of PMX B and the ability of controlled drug release. Full article
(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 3.0)
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14 pages, 3203 KiB  
Article
Ultra-Short Cyclized β-Boomerang Peptides: Structures, Interactions with Lipopolysaccharide, Antibiotic Potentiator and Wound Healing
by Sheetal Sinha, Vidhya Bharathi Dhanabal, Veronica Lavanya Manivannen, Floriana Cappiello, Suet-Mien Tan and Surajit Bhattacharjya
Int. J. Mol. Sci. 2023, 24(1), 263; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms24010263 - 23 Dec 2022
Cited by 3 | Viewed by 1696
Abstract
Many antibiotics are ineffective in killing Gram-negative bacteria due to the permeability barrier of the outer-membrane LPS. Infections caused by multi-drug-resistant Gram-negative pathogens require new antibiotics, which are often difficult to develop. Antibiotic potentiators disrupt outer-membrane LPS and can assist the entry of [...] Read more.
Many antibiotics are ineffective in killing Gram-negative bacteria due to the permeability barrier of the outer-membrane LPS. Infections caused by multi-drug-resistant Gram-negative pathogens require new antibiotics, which are often difficult to develop. Antibiotic potentiators disrupt outer-membrane LPS and can assist the entry of large-scaffold antibiotics to the bacterial targets. In this work, we designed a backbone-cyclized ultra-short, six-amino-acid-long (WKRKRY) peptide, termed cWY6 from LPS binding motif of β-boomerang bactericidal peptides. The cWY6 peptide does not exhibit any antimicrobial activity; however, it is able to permeabilize the LPS outer membrane. Our results demonstrate the antibiotic potentiator activity in the designed cWY6 peptide for several conventional antibiotics (vancomycin, rifampicin, erythromycin, novobiocin and azithromycin). Remarkably, the short cWY6 peptide exhibits wound-healing activity in in vitro assays. NMR, computational docking and biophysical studies describe the atomic-resolution structure of the peptide in complex with LPS and mode of action in disrupting the outer membrane. The dual activities of cWY6 peptide hold high promise for further translation to therapeutics. Full article
(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 3.0)
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17 pages, 1249 KiB  
Article
Structure–Activity Relationship of New Chimeric Analogs of Mastoparan from the Wasp Venom Paravespula lewisii
by Jarosław Ruczyński, Brygida Parfianowicz, Piotr Mucha, Katarzyna Wiśniewska, Lidia Piechowicz and Piotr Rekowski
Int. J. Mol. Sci. 2022, 23(15), 8269; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23158269 - 27 Jul 2022
Cited by 1 | Viewed by 1735
Abstract
Mastoparan (MP) is an antimicrobial cationic tetradecapeptide with the primary structure INLKALAALAKKIL-NH2. This amphiphilic α-helical peptide was originally isolated from the venom of the wasp Paravespula lewisii. MP shows a variety of biological activities, such as inhibition of the [...] Read more.
Mastoparan (MP) is an antimicrobial cationic tetradecapeptide with the primary structure INLKALAALAKKIL-NH2. This amphiphilic α-helical peptide was originally isolated from the venom of the wasp Paravespula lewisii. MP shows a variety of biological activities, such as inhibition of the growth of Gram-positive and Gram-negative bacteria, as well as hemolytic activity and activation of mast cell degranulation. Although MP appears to be toxic, studies have shown that its analogs have a potential therapeutic application as antimicrobial, antiviral and antitumor agents. In the present study we have designed and synthesized several new chimeric mastoparan analogs composed of MP and other biologically active peptides such as galanin, RNA III inhibiting peptide (RIP) or carrying benzimidazole derivatives attached to the ε-amino side group of Lys residue. Next, we compared their antimicrobial activity against three reference bacterial strains and conformational changes induced by membrane-mimic environments using circular dichroism (CD) spectroscopy. A comparative analysis of the relationship between the activity of peptides and the structure, as well as the calculated physicochemical parameters was also carried out. As a result of our structure–activity study, we have found two analogs of MP, MP-RIP and RIP-MP, with interesting properties. These two analogs exhibited a relatively high antibacterial activity against S. aureus compared to the other MP analogs, making them a potentially attractive target for further studies. Moreover, a comparative analysis of the relationship between peptide activity and structure, as well as the calculated physicochemical parameters, may provide information that may be useful in the design of new MP analogs. Full article
(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 3.0)
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14 pages, 9960 KiB  
Article
Is It Possible to Find an Antimicrobial Peptide That Passes the Membrane Bilayer with Minimal Force Resistance? An Attempt at a Predictive Approach by Molecular Dynamics Simulation
by Ilya V. Likhachev, Nikolay K. Balabaev and Oxana V. Galzitskaya
Int. J. Mol. Sci. 2022, 23(11), 5997; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23115997 - 26 May 2022
Cited by 2 | Viewed by 1326
Abstract
There is still no answer to the mechanism of penetration of AMP peptides through the membrane bilayer. Several mechanisms for such a process have been proposed. It is necessary to understand whether it is possible, using the molecular dynamics method, to determine the [...] Read more.
There is still no answer to the mechanism of penetration of AMP peptides through the membrane bilayer. Several mechanisms for such a process have been proposed. It is necessary to understand whether it is possible, using the molecular dynamics method, to determine the ability of peptides of different compositions and lengths to pass through a membrane bilayer. To explain the passage of a peptide through a membrane bilayer, a method for preparing a membrane phospholipid bilayer was proposed, and 656 steered molecular dynamics calculations were carried out for pulling 7 amyloidogenic peptides with antimicrobial potential, and monopeptides (homo-repeats consisting of 10 residues of the same amino acid: Poly (Ala), Poly (Leu), Poly (Met), Poly (Arg), and Poly (Glu)) with various sequences through the membrane. Among the 15 studied peptides, the peptides exhibiting the least force resistance when passing through the bilayer were found, and the maximum reaction occurred at the boundary of the membrane bilayer entry. We found that the best correlation between the maximum membrane reaction force and the calculated parameters corresponds to the instability index (the correlation coefficient is above 0.9). One of the interesting results of this study is that the 10 residue amyloidogenic peptides and their extended peptides, with nine added residue cell-penetrating peptides and four residue linkers, both with established antimicrobial activity, have the same bilayer resistance force. All calculated data are summarized and posted on the server. Full article
(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 3.0)
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21 pages, 6761 KiB  
Article
Multiple Antimicrobial Effects of Hybrid Peptides Synthesized Based on the Sequence of Ribosomal S1 Protein from Staphylococcus aureus
by Sergey V. Kravchenko, Pavel A. Domnin, Sergei Y. Grishin, Alexander V. Panfilov, Viacheslav N. Azev, Leila G. Mustaeva, Elena Y. Gorbunova, Margarita I. Kobyakova, Alexey K. Surin, Anna V. Glyakina, Roman S. Fadeev, Svetlana A. Ermolaeva and Oxana V. Galzitskaya
Int. J. Mol. Sci. 2022, 23(1), 524; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23010524 - 04 Jan 2022
Cited by 11 | Viewed by 3106
Abstract
The need to develop new antimicrobial peptides is due to the high resistance of pathogenic bacteria to traditional antibiotics now and in the future. The creation of synthetic peptide constructs is a common and successful approach to the development of new antimicrobial peptides. [...] Read more.
The need to develop new antimicrobial peptides is due to the high resistance of pathogenic bacteria to traditional antibiotics now and in the future. The creation of synthetic peptide constructs is a common and successful approach to the development of new antimicrobial peptides. In this work, we use a simple, flexible, and scalable technique to create hybrid antimicrobial peptides containing amyloidogenic regions of the ribosomal S1 protein from Staphylococcus aureus. While the cell-penetrating peptide allows the peptide to enter the bacterial cell, the amyloidogenic site provides an antimicrobial effect by coaggregating with functional bacterial proteins. We have demonstrated the antimicrobial effects of the R23F, R23DI, and R23EI hybrid peptides against Staphylococcus aureus, methicillin-resistant S. aureus (MRSA), Pseudomonas aeruginosa, Escherichia coli, and Bacillus cereus. R23F, R23DI, and R23EI can be used as antimicrobial peptides against Gram-positive and Gram-negative bacteria resistant to traditional antibiotics. Full article
(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 3.0)
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