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Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure.

Authors
  • Strub, J M
  • Hubert, P
  • Nullans, G
  • Aunis, D
  • Metz-Boutigue, M H
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Feb 05, 1996
Volume
379
Issue
3
Pages
273–278
Identifiers
PMID: 8603705
Source
Medline
License
Unknown

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.

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