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Amphiphilic α-Helical Antimicrobial Peptides and Their Structure / Function Relationships

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To facilitate microbial membrane invasion, amphiphilic α-helical antimicrobial peptides (α-AMPs) show a spatial segregation of hydrophobic and hydrophilic residues about the α-helical long axis. Here we discuss potential mechanisms by which these peptides are able to disrupt membrane structure and the structural characteristics, which are required for function.
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Keywords: amphiphilicity; antimicrobial peptides; microbial membranes

Document Type: Review Article

Affiliations: Deans Office, Faculty of Science, University of Central Lancashire, Preston, PR1 2HE, UK.

Publication date: 01 January 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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