A comparative study on the structure and function of a cytolytic α‐helical peptide and its antimicrobial β‐sheet diastereomer

Volume: 259, Issue: 1-2, Pages: 360 - 369
Published: Jan 1, 1999
Abstract
Antimicrobial peptides which adopt mainly or only β‐sheet structures have two or more disulfide bonds stabilizing their structure. The disruption of the disulfide bonds results in most cases in a large decrease in their antimicrobial activity. In the present study we examined the effect of d ‐amino acids incorporation on the structure and function of a cytolytic α‐helical peptide which acts on erythrocytes and bacteria. The influence of a single...
Paper Details
Title
A comparative study on the structure and function of a cytolytic α‐helical peptide and its antimicrobial β‐sheet diastereomer
Published Date
Jan 1, 1999
Volume
259
Issue
1-2
Pages
360 - 369
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