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

Abstract:

: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 alpha-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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Storici P,Scocchi M,Tossi A,Gennaro R,Zanetti M

doi

10.1016/0014-5793(94)80214-9

subject

Has Abstract

pub_date

1994-01-17 00:00:00

pages

303-7

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)80214-9

journal_volume

337

pub_type

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