Structure-Antibacterial Activity Relationship of Cecropin A Derivatives
To investigate the effect of net positive charge, α-helicity and hydrophobicity of the peptides on antibacterial activity, we designed three kinds of cecropin A (CA) derivatives. Compared to CA, F3 with the highest net positive charge exhibited similar or slightly weaker antibacterial activity (MIC: 3.13∼6.25 μM). F1 showed lower antibacterial activity than that of F3, even though it has higher hydrophobicity and α-helicity than F3. This result indicates that the net positive charge of cecropin A-like peptides appears to be a more important factor in antibacterial activity than α-helicity and hydrophobicity. The two peptides F1 and F2 possessed almost similar antibacterial activity, but F2 showed very lower activity in the membrane disruption than F1, suggesting other factors are involved in the antibacterial activity of the peptides as well as peptide-lipid interaction.
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Document Type: Review Article
Publication date: 2002-12-01
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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.