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Review
. 2020 Sep 24;21(19):7047.
doi: 10.3390/ijms21197047.

A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides

Katrina Browne  1 , Sudip Chakraborty  1 , Renxun Chen  1 , Mark Dp Willcox  2 , David StClair Black  1 , William R Walsh  3 , Naresh Kumar  1
Affiliations
Review

A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides

Katrina Browne et al. Int J Mol Sci. .

Abstract

Antimicrobial resistance is a multifaceted crisis, imposing a serious threat to global health. The traditional antibiotic pipeline has been exhausted, prompting research into alternate antimicrobial strategies. Inspired by nature, antimicrobial peptides are rapidly gaining attention for their clinical potential as they present distinct advantages over traditional antibiotics. Antimicrobial peptides are found in all forms of life and demonstrate a pivotal role in the innate immune system. Many antimicrobial peptides are evolutionarily conserved, with limited propensity for resistance. Additionally, chemical modifications to the peptide backbone can be used to improve biological activity and stability and reduce toxicity. This review details the therapeutic potential of peptide-based antimicrobials, as well as the challenges needed to overcome in order for clinical translation. We explore the proposed mechanisms of activity, design of synthetic biomimics, and how this novel class of antimicrobial compound may address the need for effective antibiotics. Finally, we discuss commercially available peptide-based antimicrobials and antimicrobial peptides in clinical trials.

Keywords: antibiotic-resistance; antimicrobial activity; antimicrobial peptides; cationic peptides; clinical translation; peptide-based therapies.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
A summary of events in the antibiotic-resistance timeline. WHO, World Health Organization; WWI/II, World War I/II.
Figure 2
Figure 2
Mechanistic targets of antibiotics and antimicrobial peptides.
Figure 3
Figure 3
Three-dimensional conformations of natural antimicrobial peptides. Sourced from the Protein Data Bank (https://www.rscb.org). (A) LL-37 (Homo sapiens) [26]. (B) Magainin-2 (Xenopus laevis) [27]. (C) RTD-1 (Rhesus macaque) [28]. (D) Melittin (Apis mellifera) [29]. (E) TPP3 (Solanum lycopersicum) [30]. (F) Bacteriocin AS-48 (Enterococcus faecalis) [31].
Figure 3
Figure 3
Three-dimensional conformations of natural antimicrobial peptides. Sourced from the Protein Data Bank (https://www.rscb.org). (A) LL-37 (Homo sapiens) [26]. (B) Magainin-2 (Xenopus laevis) [27]. (C) RTD-1 (Rhesus macaque) [28]. (D) Melittin (Apis mellifera) [29]. (E) TPP3 (Solanum lycopersicum) [30]. (F) Bacteriocin AS-48 (Enterococcus faecalis) [31].
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