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

FEBS Letters

Strub, Jean-Marc¹  Hubert, Pierre¹  Nullans, Gérard¹  Metz-Boutigue, Marie-Hélène¹  Aunis, Dominique¹ 

[1] Institut National de la Santé et de la Recherche Médicale, Unité 338 de Biologie de la Communication Cellulaire, 5 rue Blaise Pascal, 67084 Strasbourg, France

关键词: Bovine adrenal medulla;    Chromaffin granule;    Chromogranin;    Secretogranin;    Cecropin;    Antibacterial peptide;    CGA;    chromogranin A;    CGB;    chromogranin B/secretogranin I;    CGC;    chromogranin C/secretogranin II;    PMAP-37;    pig myeloid antibacterial peptide;   

DOI  :  10.1016/0014-5793(95)01529-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown