Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA

FEBS Letters

Zanetti, Margherita³  Gennaro, Renato²  Scocchi, Marco¹  Tossi, Alessandro¹  Storici, Paola³ 

[1] Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Université di Trieste, I-34127 Trieste, Italy;Dipartimento di Scienze e Tecnologie Biomediche, Università di Udine, I-33100 Udine, Italy;Laboratorio Nazionale Consorzio Interuniversitario Biotecnologie, AREA Science Park, Padriciano 99, I-34012 Trieste, Italy

关键词: Antibacterial peptide;    cDNA;    Amphipathic helix;    Cathelin;    Myeloid cells;   

DOI  :  10.1016/0014-5793(94)80214-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Several myeloid precursors of antibacterial peptides have recently been shown to share homologous pre- and pro-regions. Taking advantage of this homology, a novel cDNA was cloned from pig bone marrow RNA. This encodes a 166-residue polypeptide with highly conserved pre- (29 residues) and pro- (101 residues) sequences, followed by a unique, 36-residue C-terminal sequence. Structure analyses of this C-terminal region have identified a highly cationic sequence predicted to adopt an amphipathic α-helical conformation. A peptide corresponding to this sequence was chemically synthesized and shown to arrest the growth of both Gram-positive and Gram-negative bacteria. At least for Escherichia coli, the activity of this peptide appears to be mediated by its ability to permeabilize the bacterial membranes.

【 授权许可】

Unknown