Abstract
Antimicrobial agents have eradicated many infectious diseases and significantly improved our living environment. However, abuse of antimicrobial agents has accelerated the emergence of multidrug-resistant microorganisms, and there is an urgent need for novel antibiotics. Antimicrobial peptides (AMPs) have attracted attention as a novel class of antimicrobial agents because AMPs efficiently kill a wide range of species, including bacteria, fungi, and viruses, via a novel mechanism of action. In addition, they are effective against pathogens that are resistant to almost all conventional antibiotics. AMPs have promising properties; they directly disrupt the functions of cellular membranes and nucleic acids, and the rate of appearance of AMP-resistant strains is very low. However, as pharmaceuticals, AMPs exhibit unfavorable properties, such as instability, hemolytic activity, high cost of production, salt sensitivity, and a broad spectrum of activity. Therefore, it is vital to improve these properties to develop novel AMP treatments. Here, we have reviewed the basic biochemical properties of AMPs and the recent strategies used to modulate these properties of AMPs to enhance their safety.
Highlights
Since the discovery of the first antibiotic, penicillin [1], public health has been significantly improved by the subsequent development of a variety of antibiotics
Antimicrobial peptides (AMPs) bind to bacterial surfaces via electrostatic interactions, some types of AMPs can directly interact with host cells and lyse them [25]
The ratio of antimicrobial activity to hemolytic activity is defined as the therapeutic index, and a high therapeutic index is necessary for avoiding hemolysis of host cells [64]
Summary
Since the discovery of the first antibiotic, penicillin [1], public health has been significantly improved by the subsequent development of a variety of antibiotics. AMPs disrupt membrane structure, inhibit protein and DNA synthesis, and repress cellular processes, including protein folding, cell wall synthesis, and metabolic turnover [20,21] Due to these diverse mechanisms of action, AMPs have strong antimicrobial activity in the nanomolar or micromolar range against a broad spectrum of microorganisms, including Gram-positive and Gram-negative bacteria, fungi, and viruses [22,23]. They are effective against pathogenic organisms that are resistant to conventional drugs [24]. AMP, antimicrobial peptide; Orn, ornithine; dF, D-isoform of phenylalanine; Thr, threonine; LPS, lipopolysaccharide; LBP, LPS-binding protein; STAMP, targeted antimicrobial peptide
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