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Review
. 2020 Apr 23;10(4):652.
doi: 10.3390/biom10040652.

Antimicrobial and Antibiofilm Peptides

Affiliations
Review

Antimicrobial and Antibiofilm Peptides

Angela Di Somma et al. Biomolecules. .

Abstract

The increasing onset of multidrug-resistant bacteria has propelled microbiology research towards antimicrobial peptides as new possible antibiotics from natural sources. Antimicrobial peptides are short peptides endowed with a broad range of activity against both Gram-positive and Gram-negative bacteria and are less prone to trigger resistance. Besides their activity against planktonic bacteria, many antimicrobial peptides also show antibiofilm activity. Biofilms are ubiquitous in nature, having the ability to adhere to virtually any surface, either biotic or abiotic, including medical devices, causing chronic infections that are difficult to eradicate. The biofilm matrix protects bacteria from hostile environments, thus contributing to the bacterial resistance to antimicrobial agents. Biofilms are very difficult to treat, with options restricted to the use of large doses of antibiotics or the removal of the infected device. Antimicrobial peptides could represent good candidates to develop new antibiofilm drugs as they can act at different stages of biofilm formation, on disparate molecular targets and with various mechanisms of action. These include inhibition of biofilm formation and adhesion, downregulation of quorum sensing factors, and disruption of the pre-formed biofilm. This review focuses on the proprieties of antimicrobial and antibiofilm peptides, with a particular emphasis on their mechanism of action, reporting several examples of peptides that over time have been shown to have activity against biofilm.

Keywords: antimicrobial peptides; biofilm; biofilm formation inhibition; mechanism of action; resistance.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Antimicrobial peptides from the Antimicrobial Peptide Database (total of 3180). Data updated to 10th April 2020.
Figure 2
Figure 2
Antimicrobial peptide classes: α-helical, β-sheet, loop, and extended. Structures were generated by CHIMERA software [31]. PDB codes: (a) 2MAG, Magainin-2; (b) 2K6O, LL-37; (c) 1KJ5, Human β-defensin-3; (d) 1PG1, Protegrin I; (e) 1G89, Indolicidin; (f) 5XO3, Thanatin; (g) 1D6X, Tritrpticin; (h) 1LFC, Lactoferricin B.
Figure 3
Figure 3
Biofilm formation consists on attachment, proliferation, mutation and detachment stages, which can be inhibited by antimicrobial peptides

References

    1. Fleming A. On the antibacterial action of cultures of a penicillium, with special reference to their use in the isolation of B. influenzae. Br. J. Exp. Pathol. 1929;10:226. doi: 10.1093/clinids/2.1.129. - DOI - PMC - PubMed
    1. Zaffiri L., Gardner J., Toledo-Pereyra L.H. History of antibiotics. From salvarsan to cephalosporins. J. Investig. Surg. 2012;25:67–77. doi: 10.3109/08941939.2012.664099. - DOI - PubMed
    1. Bentley R. Different roads to discovery; Prontosil (hence sulfa drugs) and penicillin (hence β-lactams) J. Ind. Microbiol. Biotechnol. 2009;36:775–786. doi: 10.1007/s10295-009-0553-8. - DOI - PubMed
    1. Davies J. Where have all the antibiotics gone? Can. J. Infect. Dis. Med Microbiol. 2006;17:287–290. doi: 10.1155/2006/707296. - DOI - PMC - PubMed
    1. Katz M.L., Mueller L.V., Polyakov M., Weinstock S.F. Where have all the antibiotic patents gone? Nat. Biotechnol. 2006;24:1529. doi: 10.1038/nbt1206-1529. - DOI - PubMed

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