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XB-ART-25455
FEBS Lett 1990 Nov 12;2741-2:151-5.
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All-D-magainin: chirality, antimicrobial activity and proteolytic resistance.

Bessalle R , Kapitkovsky A , Gorea A , Shalit I , Fridkin M .


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.

PubMed ID: 2253768
Article link: FEBS Lett


Species referenced: Xenopus
Genes referenced: magainins