title: All-D-magainin: chirality, antimicrobial activity and proteolytic resistance.
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.
authors: Department of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.
authors: R
authors: R
authors: Bessalle
authors: A
authors: A
authors: Kapitkovsky
authors: A
authors: A
authors: Gorea
authors: I
authors: I
authors: Shalit
authors: M
authors: M
authors: Fridkin
mesh_terms: D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D002918:Chymotrypsin; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D007202:Indicators and Reagents; D054806:Magainins; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D011487:Protein Conformation; D013237:Stereoisomerism; D014357:Trypsin; D029867:Xenopus Proteins
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D007202:Indicators and Reagents; D054806:Magainins; D010446:Peptide Fragments; D010455:Peptides; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus; D002918:Chymotrypsin; D014357:Trypsin