Discovery and Multifunctionality of Anti-microbial Peptides

A special issue of Antibiotics (ISSN 2079-6382). This special issue belongs to the section "Antimicrobial Peptides".

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 22889

Special Issue Editors

CNRS, Aix-Marseille University, Centrale Marseille, iSm2, 13013 Marseille, France
Interests: mycotoxins; fungal metabolites; antimicrobial; anticancer; antinflammatory; antioxidant
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Guest Editor
Aix Marseille Université, CNRS, iSm2 UMR 7313, 13397 Marseille, France
Interests: natural antimicrobial molecule; ribosomally synthesized and post-translationally modified peptides; human gut microbiome; human gut symbiont producing antimicrobial peptides

E-Mail Website
Guest Editor
Aix Marseille Université, CNRS, iSm2 UMR 7313, 13397 Marseille, France
Interests: natural antimicrobial molecule; ribosomally synthesized and post-translationally modified peptides; human gut microbiome; human gut symbiont producing antimicrobial peptides

Special Issue Information

Dear Colleagues,

According to the World Health Organization (WHO), “we are heading towards a post-antibiotic era in which common infections and minor injuries can once again kill”. Indeed, antibiotic resistance is dangerously rising worldwide, threatening our ability to cure common infectious diseases. In this context, there is an urgent need to find molecules active against pathogenic microorganisms, including resistant ones. Antimicrobial peptides (AMP) seem to be a good alternative to conventional antibiotics. Indeed, contrarily to conventional antibiotics that inhibit intracellular enzymes or processes, most AMP target the bacterial membrane, which makes them: i) active against strains already resistant to conventional antibiotics and ii) less prompt to cause resistance. Contrarily to conventional antibiotics, AMP can stimulate tissue regeneration and modulate the immune system, in addition to their antimicrobial activity, which makes them able to treat infections not only by directly killing the pathogenic microorganisms but also by helping the host to cure itself. Some AMP are furthermore shown to possess antitumor activity, allowing their potential use to treat cancer. Finally, AMP can be used to functionalize materials and surfaces, conferring them new properties.

For this Topic Collection entitled “Discovery and MultiFunctionality of Anti-Microbial Peptides”, we invite authors to submit articles covering all aspects of this theme, including the discovery of new AMP and/or of new activities of already known AMP. The Topic Collection is in connection with the conference MufoPAM which took place in Marseille (France) in October 2021, and with the next conference “7th International Symposium on Antimicrobial Peptides – AMP 2022” taking place in Paris (France) in November 2022.

Dr. Marc Maresca
Prof. Josette Perrier
Dr. Michael Lafond
Guest Editors

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Keywords

  • New AMP
  • new activities
  • multifunctionality
  • antimicrobial surface & material
  • functionalized surfaces & materials
  • antibiotic resistance

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Published Papers (3 papers)

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Research

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16 pages, 1908 KiB  
Article
Synthesis of Second-Generation Analogs of Temporin-SHa Peptide Having Broad-Spectrum Antibacterial and Anticancer Effects
by Arif Iftikhar Khan, Shahzad Nazir, Muhammad Nadeem ul Haque, Rukesh Maharjan, Farooq-Ahmad Khan, Hamza Olleik, Elise Courvoisier-Dezord, Marc Maresca and Farzana Shaheen
Antibiotics 2024, 13(8), 758; https://doi.org/10.3390/antibiotics13080758 - 11 Aug 2024
Cited by 2 | Viewed by 1733
Abstract
Antimicrobial peptides (AMPs) are a promising class of therapeutic alternatives with broad-spectrum activity against resistant pathogens. Small AMPs like temporin-SHa (1) and its first-generation analog [G10a]-SHa (2) possess notable efficacy against Gram-positive and Gram-negative bacteria. In an effort to [...] Read more.
Antimicrobial peptides (AMPs) are a promising class of therapeutic alternatives with broad-spectrum activity against resistant pathogens. Small AMPs like temporin-SHa (1) and its first-generation analog [G10a]-SHa (2) possess notable efficacy against Gram-positive and Gram-negative bacteria. In an effort to further improve this antimicrobial activity, second-generation analogs of 1 were synthesised by replacing the natural glycine residue at position-10 of the parent molecule with atypical amino acids, such as D-Phenylalanine, D-Tyrosine and (2-Naphthyl)-D-alanine, to study the effect of hydrophobicity on antimicrobial efficacy. The resultant analogs (36) emerged as broad-spectrum antibacterial agents. Notably, the [G10K]-SHa analog (4), having a lysine substitution, demonstrated a 4-fold increase in activity against Gram-negative (Enterobacter cloacae DSM 30054) and Gram-positive (Enterococcus faecalis DSM 2570) bacteria relative to the parent peptide (1). Among all analogs, [G10f]-SHa peptide (3), featuring a D-Phe substitution, showed the most potent anticancer activity against lung cancer (A549), skin cancer (MNT-1), prostate cancer (PC-3), pancreatic cancer (MiaPaCa-2) and breast cancer (MCF-7) cells, achieving an IC50 value in the range of 3.6–6.8 µM; however, it was also found to be cytotoxic against normal cell lines as compared to [G10K]-SHa (4). Peptide 4 also possessed good anticancer activity but was found to be less cytotoxic against normal cell lines as compared to 1 and 3. These findings underscore the potential of second-generation temporin-SHa analogs, especially analog 4, as promising leads to develop new broad-spectrum antibacterial and anticancer agents. Full article
(This article belongs to the Special Issue Discovery and Multifunctionality of Anti-microbial Peptides)
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15 pages, 1738 KiB  
Article
Bioengineering the Antimicrobial Activity of Yeast by Recombinant Thanatin Production
by Sofiya O. Pipiya, Arsen M. Kudzhaev, Nisso Z. Mirzoeva, Yuliana A. Mokrushina, Rustam H. Ziganshin, Alexey S. Komlev, Polina E. Petrova, Ivan V. Smirnov, Alexander G. Gabibov, Olga V. Shamova and Stanislav S. Terekhov
Antibiotics 2023, 12(12), 1719; https://doi.org/10.3390/antibiotics12121719 - 12 Dec 2023
Cited by 2 | Viewed by 2692
Abstract
The global spread of antibiotic resistance marks the end of the era of conventional antibiotics. Mankind desires new molecular tools to fight pathogenic bacteria. In this regard, the development of new antimicrobials based on antimicrobial peptides (AMPs) is again of particular interest. AMPs [...] Read more.
The global spread of antibiotic resistance marks the end of the era of conventional antibiotics. Mankind desires new molecular tools to fight pathogenic bacteria. In this regard, the development of new antimicrobials based on antimicrobial peptides (AMPs) is again of particular interest. AMPs have various mechanisms of action on bacterial cells. Moreover, AMPs have been reported to be efficient in preclinical studies, demonstrating a low level of resistance formation. Thanatin is a small, beta-hairpin antimicrobial peptide with a bacterial-specific mode of action, predetermining its low cytotoxicity toward eukaryotic cells. This makes thanatin an exceptional candidate for new antibiotic development. Here, a microorganism was bioengineered to produce an antimicrobial agent, providing novel opportunities in antibiotic research through the directed creation of biocontrol agents. The constitutive heterologous production of recombinant thanatin (rThan) in the yeast Pichia pastoris endows the latter with antibacterial properties. Optimized expression and purification conditions enable a high production level, yielding up to 20 mg/L of rThan from the culture medium. rThan shows a wide spectrum of activity against pathogenic bacteria, similarly to its chemically synthesized analogue. The designed approach provides new avenues for AMP engineering and creating live biocontrol agents to fight antibiotic resistance. Full article
(This article belongs to the Special Issue Discovery and Multifunctionality of Anti-microbial Peptides)
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Review

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21 pages, 357 KiB  
Review
Overview of Global Trends in Classification, Methods of Preparation and Application of Bacteriocins
by Maria Zimina, Olga Babich, Alexander Prosekov, Stanislav Sukhikh, Svetlana Ivanova, Margarita Shevchenko and Svetlana Noskova
Antibiotics 2020, 9(9), 553; https://doi.org/10.3390/antibiotics9090553 - 28 Aug 2020
Cited by 131 | Viewed by 16644
Abstract
This paper summarizes information about the division of bacteriocins into classes (Gram-negative bacteria, Gram-positive bacteria, and archaea). Methods for producing bacteriocins have been studied. It is known that bacteriocins, most successfully used today are products of secondary metabolism of lactic acid bacteria. It [...] Read more.
This paper summarizes information about the division of bacteriocins into classes (Gram-negative bacteria, Gram-positive bacteria, and archaea). Methods for producing bacteriocins have been studied. It is known that bacteriocins, most successfully used today are products of secondary metabolism of lactic acid bacteria. It is established that the main method of bacteriocin research is PCR analysis, which makes it possible to quickly and easily identify the presence of bacteriocin encoding genes. The mechanism of cytotoxic action of bacteriocins has been studied. It is proved that the study of cytotoxic (antitumor) activity in laboratory conditions will lead to the clinical use of bacteriocins for cancer treatment in the near future. It is established that the incorporation of bacteriocins into nanoparticles and targeted delivery to areas of infection may soon become an effective treatment method. The delivery of bacteriocins in a concentrated form, such as encapsulated in nanoparticles, will increase their effectiveness and minimize potential toxic side effects. The analysis of publications on this topic confirmed that diverse research on bacteriocins is relevant. Full article
(This article belongs to the Special Issue Discovery and Multifunctionality of Anti-microbial Peptides)
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