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Creation of New Antimicrobial Peptides 2.0

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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 (31 August 2021) | Viewed by 19477

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Prof. Dr. Oxana V. Galzitskaya

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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
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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

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Keywords

anti-infective agents
antimicrobial peptide
bacterial infection
induced resistance

Published Papers (6 papers)

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Research

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18 pages, 5225 KiB

Open AccessArticle

Isolation of Persister Cells of Bacillus subtilis and Determination of Their Susceptibility to Antimicrobial Peptides

by Shiqi Liu, Stanley Brul and Sebastian A. J. Zaat

Int. J. Mol. Sci. 2021, 22(18), 10059; https://doi.org/10.3390/ijms221810059 - 17 Sep 2021

Cited by 8 | Viewed by 3151

Abstract

Persister cells are growth-arrested subpopulations that can survive possible fatal environments and revert to wild types after stress removal. Clinically, persistent pathogens play a key role in antibiotic therapy failure, as well as chronic, recurrent, and antibiotic-resilient infections. In general, molecular and physiological research on persister cells formation and compounds against persister cells are much desired. In this study, we firstly demonstrated that the spore forming Gram-positive model organism Bacillus subtilis can be used to generate persister cells during exposure to antimicrobial compounds. Interestingly, instead of exhibiting a unified antibiotic tolerance profile, different number of persister cells and spores were quantified in various stress conditions. qPCR results also indicated that differential stress responses are related to persister formation in various environmental conditions. We propose, for the first time to the best of our knowledge, an effective method to isolate B. subtilis persister cells from a population using fluorescence-activated cell sorting (FACS), which makes analyzing persister populations feasible. Finally, we show that alpha-helical cationic antimicrobial peptides SAAP-148 and TC-19, derived from human cathelicidin LL-37 and human thrombocidin-1, respectively, have high efficiency against both B. subtilis vegetative cells and persisters, causing membrane permeability and fluidity alteration. In addition, we confirm that in contrast to persister cells, dormant B. subtilis spores are not susceptible to the antimicrobial peptides. Full article

(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 2.0)

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15 pages, 32862 KiB

Open AccessArticle

Key Physicochemical Determinants in the Antimicrobial Peptide RiLK1 Promote Amphipathic Structures

by Lucia Falcigno, Gabriella D’Auria, Gianna Palmieri, Marta Gogliettino, Bruna Agrillo, Rosarita Tatè, Principia Dardano, Luigi Nicolais and Marco Balestrieri

Int. J. Mol. Sci. 2021, 22(18), 10011; https://doi.org/10.3390/ijms221810011 - 16 Sep 2021

Cited by 5 | Viewed by 2355

Abstract

Antimicrobial peptides (AMPs) represent a skilled class of new antibiotics, due to their broad range of activity, rapid killing, and low bacterial resistance. Many efforts have been made to discover AMPs with improved performances, i.e., high antimicrobial activity, low cytotoxicity against human cells, stability against proteolytic degradation, and low costs of production. In the design of new AMPs, several physicochemical features, such as hydrophobicity, net positive charge, propensity to assume amphipathic conformation, and self-assembling properties, must be considered. Starting from the sequence of the dodecapeptide 1018-K6, we designed a new 10-aminoacid peptide, namely RiLK1, which is highly effective against both fungi and Gram-positive and -negative bacteria at low micromolar concentrations without causing human cell cytotoxicity. In order to find the structural reasons explaining the improved performance of RiLK1 versus 1018-K6, a comparative analysis of the two peptides was carried out with a combination of CD, NMR, and fluorescence spectroscopies, while their self-assembling properties were analyzed by optical and atomic force microscopies. Interestingly, the different spectroscopic and microscopic profiles exhibited by the two peptides, including the propensity of RiLK1 to adopt helix arrangements in contrast to 1018-K6, could explain the improved bactericidal, antifungal, and anti-biofilm activities shown by the new peptide against a panel of food pathogens. Full article

(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 2.0)

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23 pages, 5663 KiB

Open AccessArticle

Is It Possible to Create Antimicrobial Peptides Based on the Amyloidogenic Sequence of Ribosomal S1 Protein of P. aeruginosa?

by Sergei Y. Grishin, Pavel A. Domnin, Sergey V. Kravchenko, Viacheslav N. Azev, Leila G. Mustaeva, Elena Y. Gorbunova, Margarita I. Kobyakova, Alexey K. Surin, Maria A. Makarova, Stanislav R. Kurpe, Roman S. Fadeev, Alexey S. Vasilchenko, Victoria V. Firstova, Svetlana A. Ermolaeva and Oxana V. Galzitskaya

Int. J. Mol. Sci. 2021, 22(18), 9776; https://doi.org/10.3390/ijms22189776 - 10 Sep 2021

Cited by 10 | Viewed by 2983

Abstract

The development and testing of new antimicrobial peptides (AMPs) represent an important milestone toward the development of new antimicrobial drugs that can inhibit the growth of pathogens and multidrug-resistant microorganisms such as Pseudomonas aeruginosa, Gram-negative bacteria. Most AMPs achieve these goals through mechanisms that disrupt the normal permeability of the cell membrane, which ultimately leads to the death of the pathogenic cell. Here, we developed a unique combination of a membrane penetrating peptide and peptides prone to amyloidogenesis to create hybrid peptide: “cell penetrating peptide + linker + amyloidogenic peptide”. We evaluated the antimicrobial effects of two peptides that were developed from sequences with different propensities for amyloid formation. Among the two hybrid peptides, one was found with antibacterial activity comparable to antibiotic gentamicin sulfate. Our peptides showed no toxicity to eukaryotic cells. In addition, we evaluated the effect on the antimicrobial properties of amino acid substitutions in the non-amyloidogenic region of peptides. We compared the results with data on the predicted secondary structure, hydrophobicity, and antimicrobial properties of the original and modified peptides. In conclusion, our study demonstrates the promise of hybrid peptides based on amyloidogenic regions of the ribosomal S1 protein for the development of new antimicrobial drugs against P. aeruginosa. Full article

(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 2.0)

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17 pages, 4750 KiB

Open AccessArticle

Potent Activity of Hybrid Arthropod Antimicrobial Peptides Linked by Glycine Spacers

by Miray Tonk, James J. Valdés, Alejandro Cabezas-Cruz and Andreas Vilcinskas

Int. J. Mol. Sci. 2021, 22(16), 8919; https://doi.org/10.3390/ijms22168919 - 18 Aug 2021

Cited by 7 | Viewed by 3086

Abstract

Arthropod antimicrobial peptides (AMPs) offer a promising source of new leads to address the declining number of novel antibiotics and the increasing prevalence of multidrug-resistant bacterial pathogens. AMPs with potent activity against Gram-negative bacteria and distinct modes of action have been identified in insects and scorpions, allowing the discovery of AMP combinations with additive and/or synergistic effects. Here, we tested the synergistic activity of two AMPs, from the dung beetle Copris tripartitus (CopA3) and the scorpion Heterometrus petersii (Hp1090), against two strains of Escherichia coli. We also tested the antibacterial activity of two hybrid peptides generated by joining CopA3 and Hp1090 with linkers comprising two (InSco2) or six (InSco6) glycine residues. We found that CopA3 and Hp1090 acted synergistically against both bacterial strains, and the hybrid peptide InSco2 showed more potent bactericidal activity than the parental AMPs or InSco6. Molecular dynamics simulations revealed that the short linker stabilizes an N-terminal 3₁₀-helix in the hybrid peptide InSco2. This secondary structure forms from a coil region that interacts with phosphatidylethanolamine in the membrane bilayer model. The highest concentration of the hybrid peptides used in this study was associated with stronger hemolytic activity than equivalent concentrations of the parental AMPs. As observed for CopA3, the increasing concentration of InSco2 was also cytotoxic to BHK-21 cells. We conclude that AMP hybrids linked by glycine spacers display potent antibacterial activity and that the cytotoxic activity can be modulated by adjusting the nature of the linker peptide, thus offering a strategy to produce hybrid peptides as safe replacements or adjuncts for conventional antibiotic therapy. Full article

(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 2.0)

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14 pages, 4668 KiB

Open AccessArticle

Identification of Amyloidogenic Regions in Pseudomonas aeruginosa Ribosomal S1 Protein

by Sergei Y. Grishin, Ulyana F. Dzhus, Anatoly S. Glukhov, Olga M. Selivanova, Alexey K. Surin and Oxana V. Galzitskaya

Int. J. Mol. Sci. 2021, 22(14), 7291; https://doi.org/10.3390/ijms22147291 - 7 Jul 2021

Cited by 8 | Viewed by 2275

Abstract

Bacterial S1 protein is a functionally important ribosomal protein. It is a part of the 30S ribosomal subunit and is also able to interact with mRNA and tmRNA. An important feature of the S1 protein family is a strong tendency towards aggregation. To study the amyloidogenic properties of S1, we isolated and purified the recombinant ribosomal S1 protein of Pseudomonas aeruginosa. Using the FoldAmyloid, Waltz, Pasta 2.0, and AGGRESCAN programs, amyloidogenic regions of the protein were predicted, which play a key role in its aggregation. The method of limited proteolysis in combination with high performance liquid chromatography and mass spectrometric analysis of the products, made it possible to identify regions of the S1 protein from P. aeruginosa that are protected from the action of proteinase K, trypsin, and chymotrypsin. Sequences of theoretically predicted and experimentally identified amyloidogenic regions were used to synthesize four peptides, three of which demonstrated the ability to form amyloid-like fibrils, as shown by electron microscopy and fluorescence spectroscopy. The identified amyloidogenic sites can further serve as a basis for the development of new antibacterial peptides against the pathogenic microorganism P. aeruginosa. Full article

(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 2.0)

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Review

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13 pages, 1441 KiB

Open AccessReview

Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action

by Rachita Dash and Surajit Bhattacharjya

Int. J. Mol. Sci. 2021, 22(4), 1522; https://doi.org/10.3390/ijms22041522 - 3 Feb 2021

Cited by 51 | Viewed by 4269

Abstract

Antimicrobial peptides (AMPs) possess great potential for combating drug-resistant bacteria. Thanatin is a pathogen-inducible single-disulfide-bond-containing β-hairpin AMP which was first isolated from the insect Podisus maculiventris. The 21-residue-long thanatin displays broad-spectrum activity against both Gram-negative and Gram-positive bacteria as well as against various species of fungi. Remarkably, thanatin was found to be highly potent in inhibiting the growth of bacteria and fungi at considerably low concentrations. Although thanatin was isolated around 25 years ago, only recently has there been a pronounced interest in understanding its mode of action and activity against drug-resistant bacteria. In this review, multiple modes of action of thanatin in killing bacteria and in vivo activity, therapeutic potential are discussed. This promising AMP requires further research for the development of novel molecules for the treatment of infections caused by drug resistant pathogens. Full article

(This article belongs to the Special Issue Creation of New Antimicrobial Peptides 2.0)

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