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Antibacterial activity of secretolytin, a chromogranin B‐derived peptide (614–626), is correlated with peptide structure
Author(s) -
Strub Jean-Marc,
Hubert Pierre,
Nullans Gérard,
Aunis Dominique,
Metz-Boutigue Marie-Hélène
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01529-9
Subject(s) - peptide , chromogranin a , antibacterial activity , peptide sequence , antibacterial agent , extracellular , chemistry , lytic cycle , biochemistry , biology , bacteria , immunology , antibiotics , genetics , immunohistochemistry , virus , gene
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.