Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure.
Amongst the chromogranin B (CGB) derived fragments naturally generated in bovine chromaffin granules and detected in the extracellular space, we recently identified a major peptide corresponding to the 614-626 sequence of CGB. This peptide, named secretolytin, shared an interesting sequence homology with the lytic domain of cecropins and displayed a potent antibacterial activity. The aim of the present study was to determine the structural features of secretolytin necessary for this biological activity. Our results suggest that an alpha-helical amphipathic structure common to secretolytin, cecropins and pig myeloid antibacterial peptide may account for the antibacterial activity.
Strub
J M
JM
Institut National de la Santé et de la Recherche Médicale, Unité 338 de Biologie de la Communication Cellulaire, Strasbourg, France.
Hubert
P
P
Nullans
G
G
Aunis
D
D
Metz-Boutigue
M H
MH
D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D001407:Bacillus / Q000187:drug effects; D001483:Base Sequence; D002417:Cattle; D053378:Chromogranin B; D002864:Chromogranins / Q000737:chemistry* / Q000494:pharmacology; D003198:Computer Simulation; D004352:Drug Resistance, Microbial; D007301:Insect Hormones / Q000737:chemistry; D008837:Micrococcus / Q000187:drug effects; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000494:pharmacology; D016415:Sequence Alignment; D017385:Sequence Homology; D013329:Structure-Activity Relationship; D013552:Swine
D000900:Anti-Bacterial Agents; D053378:Chromogranin B; D002864:Chromogranins; D007301:Insect Hormones; D010446:Peptide Fragments; C093477:secretolytin