Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA.
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.
Storici
P
P
Laboratorio Nazionale Consorzio Interuniversitario Biotecnologie, AREA Science Park, Trieste, Italy.
Scocchi
M
M
Tossi
A
A
Gennaro
R
R
Zanetti
M
M
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D001419:Bacteria / Q000187:drug effects*; D001483:Base Sequence; D001853:Bone Marrow / Q000737:chemistry*; D002463:Cell Membrane Permeability / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D018076:DNA, Complementary / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000187:drug effects; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000235:genetics / Q000494:pharmacology; D016133:Polymerase Chain Reaction; D017433:Protein Structure, Secondary; D011506:Proteins / Q000138:chemical synthesis* / Q000235:genetics / Q000494:pharmacology; D013552:Swine
D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; C085474:PMAP-36; D010455:Peptides; D011506:Proteins