Lipopeptides like daptomycin, surfactin, polymyxin, etc. have antimicrobial properties. They bind to the bacterial cells and creates pores in their cell membrane which results in cell lysis. What part or residue of bacterial cell do these lipopeptides bind?
Lipopeptides bind to lipid membrane and increase permeability of the cells of bacteria or fungus
AMPs are not ideal drugs: they are far larger than typical druglike molecules, tend to be expensive to synthesize, and are prone to peptidase degradation when used internally . This suggests that the best case for a drug based on a natural linear AMP is a topical antibiotic, although daptomycin, which, (even though it is somewhat toxic to human cells), has been approved by the Food and Drug Administration (FDA) for therapeutic application in systemic and life-threatening infections caused by Gram-positive bacteria.
Several models have been proposed to explain the molecular mechanism of AMPs,(antimicrobial peptides) such as barrel-stave model or More recently explained by both Makovitzki and his colleagues , and Vallon-Eberhard and his colleagues.
You can review the following :
Makovitzki, A., D. Avrahami, and Y. Shai. 2006. Ultrashort antibacterial
and antifungal lipopeptides. Proc. Natl. Acad. Sci. USA.
Vallon-Eberhard, A., A. Makovitzki, ., Y. Shai. 2008. Efficient clearance of Aspergillus fumigatus in murine lungs by an ultrashort antimicrobial lipopeptide, palmitoyl-lys-ala-DAla-lys. Antimicrob. Agents Chemother.
Lipopeptides are amphipathic molecules and work in a similar manner to detergents: by integrating within and destabilizing cellular membranes. They would bind to any molecule that binds lipids, including integral membrane proteins, and lipid transfer proteins.
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