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Human Antimicrobial Peptides: Spectrum, Mode of Action and Resistance Mechanisms

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Abstract

Overuse of antibiotics is one of the important factors that contribute to developing antimicrobial resistance. Many studies have been conducted to find out promising solutions to overcome the problems. Antimicrobial peptides (AMPs) are fundamental components of human innate immunity. They have an important role in the treatment of a wide range of diseases, including cancer, allergies, and also in warding off invading pathogens. In the case of infectious disease, the AMPs exhibit broad-spectrum activity against a wide range of pathogens including Gram-positive and -negative bacteria, yeasts, fungi, and enveloped viruses. These peptides have been isolated from various sources such as microorganisms, plants, invertebrates, and vertebrates. The peptides show distinct physicochemical and structural properties but most of them are small cationic peptides with amphipathic properties. In this review, an overview of the classification, antimicrobial activities, mode of action, and mechanism of resistance of human AMPs will be provided. These peptides are categorized into three main groups. The defensins are cationic peptides containing six cysteine residues with three intramolecular disulfide bridges. In humans, two classes of defensins could be found, α-defensins and β-defensins. The second group is cathelicidins that only one AMP, LL-37, has been found in humans. This peptide is derived from proteolytic digestion of the C-terminal of human CAP18 protein. The third group is the family of histatins that are small cationic histidine-rich peptides, and mainly present in human saliva. The last two groups have random coil conformation in hydrophilic environments and α-helices in a hydrophobic environment.

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Data Availability

This review was based on data extracted from published papers available in all relevant databases without limitation up to 1st July 2020.

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Authors and Affiliations

  1. Biotechnology Research Center, Pharmaceutical Technology Institute, Mashhad University of Medical Sciences, Mashhad, Iran

    Bibi Sedigheh Fazly Bazzaz

  2. Department of Pharmaceutical Control, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran

    Bibi Sedigheh Fazly Bazzaz & Bahman Khameneh

  3. School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran

    Shabnam Seyedi & Narjes Hoseini Goki

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  1. Bibi Sedigheh Fazly Bazzaz
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  2. Shabnam Seyedi
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  3. Narjes Hoseini Goki
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BK collaborated in the original idea, concept, design, and writing and drafting the article. SS and NHG contributed with data interpretation, writing, and drafting of the article. BSFB contributed to all stages of the process and mainly participated in drafting the article, writing, and editing the final version to be published. All the authors read and approved the final version of the manuscript.

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Fazly Bazzaz, B.S., Seyedi, S., Hoseini Goki, N. et al. Human Antimicrobial Peptides: Spectrum, Mode of Action and Resistance Mechanisms. Int J Pept Res Ther 27, 801–816 (2021). https://doi.org/10.1007/s10989-020-10127-2

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