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All-D-magainin: chirality, antimicrobial activity and proteolytic resistance
R Bessalle1, A Kapitkovsky, A Gorea
1Department of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.
FEBS Letters
|November 12, 1990
Abstract:
All-D-magainin-2 was synthesized to corroborate experimentally the notion that the biological function of a surface-active peptide stems primarily from its unique amphiphilic alpha-helical structure. Indeed, the peptide exhibited antibacterial potency nearly identical to that of the all-L-enantiomer. Being highly resistant to proteolysis and non-hemolytic all-D-magainin might have considerable therapeutic importance.