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 Lettjournal_title
FEBS lettersauthors
Storici P,Scocchi M,Tossi A,Gennaro R,Zanetti Mdoi
10.1016/0014-5793(94)80214-9subject
Has Abstractpub_date
1994-01-17 00:00:00pages
303-7issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(94)80214-9journal_volume
337pub_type
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