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Current Pharmaceutical Biotechnology

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ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

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Review Article

Structure, Function, and Physicochemical Properties of Pore-forming Antimicrobial Peptides

Author(s): Narjes Hosseini Goki, Zeinab Amiri Tehranizadeh, Mohammad Reza Saberi, Bahman Khameneh* and Bibi Sedigheh Fazly Bazzaz*

Volume 25, Issue 8, 2024

Published on: 25 October, 2023

Page: [1041 - 1057] Pages: 17

DOI: 10.2174/0113892010194428231017051836

Price: $65

Open Access Journals Promotions 2
Abstract

Antimicrobial peptides (AMPs), a class of antimicrobial agents, possess considerable potential to treat various microbial ailments. The broad range of activity and rare complete bacterial resistance to AMPs make them ideal candidates for commercial development. These peptides with widely varying compositions and sources share recurrent structural and functional features in mechanisms of action. Studying the mechanisms of AMP activity against bacteria may lead to the development of new antimicrobial agents that are more potent. Generally, AMPs are effective against bacteria by forming pores or disrupting membrane barriers. The important structural aspects of cytoplasmic membranes of pathogens and host cells will also be outlined to understand the selective antimicrobial actions. The antimicrobial activities of AMPs are related to multiple physicochemical properties, such as length, sequence, helicity, charge, hydrophobicity, amphipathicity, polar angle, and also self-association. These parameters are interrelated and need to be considered in combination. So, gathering the most relevant available information will help to design and choose the most effective AMPs.

Keywords: Antimicrobial peptide, cationic peptide, structural characteristics, membrane disruption, pore formation, physicochemical properties.

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