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

Sarah   R.   Dennison; James      Wallace; Frederick      Harris; David   A.   Phoenix

doi:10.2174/0929866053406084

Abstract

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.

Keywords: antimicrobial peptides, amphiphilicity, microbial membranes

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Protein & Peptide Letters

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

Volume: 12 Issue: 1

Author(s): Sarah R. Dennison, James Wallace, Frederick Harris and David A. Phoenix

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Keywords: antimicrobial peptides, amphiphilicity, microbial membranes

Abstract: 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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Dennison R. Sarah, Wallace James, Harris Frederick and Phoenix A. David, Amphiphilic α-Helical Antimicrobial Peptides and Their Structure / Function Relationships, Protein & Peptide Letters 2005; 12 (1) . https://dx.doi.org/10.2174/0929866053406084