All-D-magainin: chirality, antimicrobial activity and proteolytic resistance.
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.
Bessalle
R
R
Department of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.
Kapitkovsky
A
A
Gorea
A
A
Shalit
I
I
Fridkin
M
M
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
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