Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides
Open Access
- 20 April 2022
- journal article
- review article
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (9) , 4558
Abstract
Global rise of infections and deaths caused by drug-resistant bacterial pathogens are among the unmet medical needs. In an age of drying pipeline of novel antibiotics to treat bacterial infections, antimicrobial peptides (AMPs) are proven to be valid therapeutics modalities. Direct in vivo applications of many AMPs could be challenging; however, works are demonstrating encouraging results for some of them. In this review article, we discussed 3-D structures of potent AMPs e.g., polymyxin, thanatin, MSI, protegrin, OMPTA in complex with bacterial targets and their mode of actions. Studies on human peptide LL37 and de novo-designed peptides are also discussed. We have focused on AMPs which are effective against drug-resistant Gram-negative bacteria. Since treatment options for the infections caused by super bugs of Gram-negative bacteria are now extremely limited. We also summarize some of the pertinent challenges in the field of clinical trials of AMPs.Keywords
This publication has 177 references indexed in Scilit:
- Structure, Dynamics, and Antimicrobial and Immune Modulatory Activities of Human LL-23 and Its Single-Residue Variants Mutated on the Basis of Homologous Primate CathelicidinsBiochemistry, 2011
- Structures of β-Hairpin Antimicrobial Protegrin Peptides in Lipopolysaccharide Membranes: Mechanism of Gram Selectivity Obtained from Solid-State Nuclear Magnetic ResonanceBiochemistry, 2011
- NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide MicellesJournal of Biological Chemistry, 2010
- Antimicrobial and Membrane Disrupting Activities of a Peptide Derived from the Human Cathelicidin Antimicrobial Peptide LL37Biophysical Journal, 2010
- Structure−Activity Relationships of Polymyxin AntibioticsJournal of Medicinal Chemistry, 2009
- Designed β-Boomerang Antiendotoxic and Antimicrobial PeptidesJournal of Biological Chemistry, 2009
- Structure, membrane orientation, mechanism, and function of pexiganan — A highly potent antimicrobial peptide designed from magaininBiochimica et Biophysica Acta (BBA) - Biomembranes, 2009
- Interactions of Lipopolysaccharide and Polymyxin Studied by NMR SpectroscopyJournal of Biological Chemistry, 2009
- Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMRProceedings of the National Academy of Sciences, 2006
- Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?Nature Reviews Microbiology, 2005