Properties / Characteristics of Antimicrobial Peptides

Abstract

Antimicrobial peptides (AMPs) are natural antibiotics, synthesized by ribosomes, with an effect on the natural immunity of animal organisms. AMPs differ in composition [sequence and type of amino acids (AAs)] and structure, which contribute to rapid lysis and have a varied spectrum of antimicrobial activity. AMPs are: peptides (Pps) with alpha-helix structure (i.e., cecropins, magainins, mellitin, etc.); cyclic Pps and ring with several cysteine residues (i.e., defensins, protegrins, etc.); Pps rich in one or another AA (i.e., proline arginine-rich PR39, histidine, glycine, etc.). Most AMPs are characterized by hydrophobic and cationic properties, adopt an amphipathic structure (alpha-helix, spiral beta or alpha-helix / spiral beta), which is essential for antimicrobial activity. AMPs have the potential for therapeutic use in medicine. One of the major concerns of life sciences research is finding new ways to enhance the body’s defense against pathogens. One way is to produce drugs based on AMPs. The AMPs are a class of small Pps that have the ability to destroy pathogens of microbial and viral origin. The mechanisms of action are known only partially and for a small number of AMPs, and the toxic action of AMPs is generally considered to be based on the induction by these molecules in the outer membrane of the pathogen of aqueous pores that facilitate nonspecific ion transfer, which ultimately leads to lysis of the target cell.