| Literature DB >> 2253768 |
R Bessalle1, A Kapitkovsky, A Gorea, I Shalit, M Fridkin.
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.Mesh：
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Year: 1990 PMID： 2253768 DOI： 10.1016/0014-5793(90)81351-n
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124