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

FEBS Letters
J M StrubM H Metz-Boutigue

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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Citations

Aug 22, 2000·The Prostate·L CarlssonM Stridsberg
Nov 26, 2010·Current Hypertension Reports·Kuixing ZhangDaniel T O'Connor
Nov 17, 2007·Acta Physiologica·M Montero-HadjadjeY Anouar
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Feb 3, 2005·Biological Reviews of the Cambridge Philosophical Society·Karen B Helle
Sep 27, 2014·Behavioural Brain Research·Daniel PeredaRicardo Borges
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Nov 26, 2009·Regulatory Peptides·Peiman ShooshtarizadehMarie-Hélène Metz-Boutigue
Sep 7, 2017·Pflügers Archiv : European journal of physiology·Karen B HelleTommaso Angelone
Jul 14, 2001·The Journal of Biological Chemistry·K LugardonM H Metz-Boutigue
Feb 7, 2001·The Journal of Biological Chemistry·K LugardonM H Metz-Boutigue

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