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All‐D‐magainin: chirality, antimicrobial activity and proteolytic resistance

Year: 1990
Type: article
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.
Source: FEBS Letters
Language: English
Subfield: Microbiology
Open Access status: bronze
OpenAlex ID: W2125829096
FWCI: 4.608
Cites: 29
Cited by: 291
Related to: 10