Antibacterial activity of secretolytin, a chromogranin B‐derived peptide (614–626), is correlated with peptide structure
- 5 February 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 379 (3) , 273-278
- https://doi.org/10.1016/0014-5793(95)01529-9
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 α-helical amphipathic structure common to secretolytin, cecropins and pig myeloid antibacterial peptide may account for the antibacterial activity.Keywords
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