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

Roberto Bessalle, Aviva Kapitkovsky, Alfred Gorea, Itamar Shalit, Mati Fridkin

Research output: Contribution to journalArticlepeer-review

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 α -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.

Original languageEnglish
Pages (from-to)151-155
Number of pages5
JournalFEBS Letters
Volume274
Issue number1-2
DOIs
StatePublished - 12 Nov 1990
Externally publishedYes

Keywords

  • All-D-magainin
  • Proteolytic stability: Clinical potential
  • Surface-activity

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