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Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide
J M Strub1, P Hubert, G Nullans
1Institut National de la Santé et de la Recherche Médicale, Unité 338 de Biologie de la Communication Cellulaire, Strasbourg, France.
Abstract:
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.