Dear Colleagues,

The polypeptide chains of peptides with antimicrobial activity generally have fifty or fewer amino acid residues. Depending on the composition of the amino acids that make up the polypeptide chain, antimicrobial peptides can have cationic, anionic, and/or aromatic charged in addition to their characteristic size and conformation. [1]. Antimicrobial peptides (AMPs) are conserved biomolecules, and are part of the defense systems of many organisms, from prokaryotes to multicellular organisms such as humans [2]. AMPs are produced by organisms as a defense mechanism against pathogenic microbes. Initial studies on defense peptides identified defensins, cecropins, retropins and cathelicidins, which have different structures and bioactivities [3]. Antimicrobial peptides can be classified according to their source (animal, plant, microbial, insect, amphibian, aquatic), and by their structure (α-helix, β-sheet, both α-helix and β-sheet, linear). They are also classified based on species rich in amino acids (especially Gly, Arg, Pro, His and Trp), and depending on their activity (e.g., antimicrobial, antiviral, antiparasitic, antifungal, anti-inflammatory and anticancer) [4]. The first reported AMP was gramicidin, isolated from Bacillus brevis in 1939. Defensin, another AMP, was isolated from rabbit leukocytes. Since the 1960s, there has been a great interest in these peptides, and more than 5000 AMPs have been reported [1]. Thus, peptides are considered promising molecules not only for application as antimicrobial therapy, but also in immunomodulatory, anticancer, antioxidant and other applications [5]. Currently, many in silico analysis methods have been helping to target peptides for antimicrobial applications. Molecular biology techniques associated with bioinformatics are also providing good results in obtaining more effective AMPs.

References

[1] Cardoso, P., Glossop, H., Meikle, T. G., Aburto-Medina, A., Conn, C. E., Sarojini, V., Valery, C. Molecular engineering of antimicrobial peptides: microbial targets, peptide motifs and translation opportunities. Biophysical Reviews, 2021, vol. 13, p.35–69, https://doi.org/10.1007/s12551-021-00784-y.

[2] Ebenhan, T., Gheysens, O., Kruger, H. G., Zeevaart, J. R., Sathekge, M. M. Antimicrobial peptides: their role as infection-selective tracers for molecular imaging. Biomed Research International, 2014, Article ID, 867381, p.1-15. https://doi.org/10.1155/2014/867381.

[3] Fjell, C. D., Hiss, J. A., Hancock, R. E. W., Schneider, G. Designing antimicrobial peptides: form follows function. Nature Reviews Drug Discovery, Vol. 11, January 2012, p.37-51. https://doi.org/10.1038/nrd3591.

[4] Huan, Y., Kong, Q., Mou, H., Yi, H. Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields. Frontiers in Microbiology, 2020, vol. 11 October 2020, p. 1-21, ID Article 582779, https://doi.org/10.3389/fmicb.2020.582779.

[5] Torres, M. D. T., Sothiselvam, S., Lu, T. K. and de la Fuente-Nunez C. Peptide Design Principles for Antimicrobial Applications. Journal of Molecular Biology, 2019, Vol. 431, p. 3547–3567, https://doi.org/10.1016/j.jmb.2018.12.015.

Dr. Hamilton Cabral
Guest Editor

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• database peptides
• therapeutic agents
• peptide design
• antimicrobial peptides
• antibiotic resistance
• therapeutic drugs