Special Issue "Bioactive Peptides and Their Antibiotic Activity"

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

Deadline for manuscript submissions: 31 December 2023 | Viewed by 900

Special Issue Editor

Associate Professor, School of Pharmaceutical Sciences of Ribeirao Preto, University of Sao Paulo, CEP, Ribeirao Preto 14040-903, SP, Brazil
Interests: bioactive peptides; cancer; natural peptides; molecular biology; proteases and proteomic
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

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.


[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

Manuscript Submission Information

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

Published Papers (1 paper)

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Tuning the Anthranilamide Peptidomimetic Design to Selectively Target Planktonic Bacteria and Biofilm
Antibiotics 2023, 12(3), 585; https://doi.org/10.3390/antibiotics12030585 - 15 Mar 2023
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There is a pressing need to develop new antimicrobials to help combat the increase in antibiotic resistance that is occurring worldwide. In the current research, short amphiphilic antibacterial and antibiofilm agents were produced by tuning the hydrophobic and cationic groups of anthranilamide peptidomimetics. [...] Read more.
There is a pressing need to develop new antimicrobials to help combat the increase in antibiotic resistance that is occurring worldwide. In the current research, short amphiphilic antibacterial and antibiofilm agents were produced by tuning the hydrophobic and cationic groups of anthranilamide peptidomimetics. The attachment of a lysine cationic group at the tail position increased activity against E. coli by >16-fold (from >125 μM to 15.6 μM) and greatly reduced cytotoxicity against mammalian cells (from ≤20 μM to ≥150 μM). These compounds showed significant disruption of preformed biofilms of S. aureus at micromolar concentrations. Full article
(This article belongs to the Special Issue Bioactive Peptides and Their Antibiotic Activity)
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