Cloning and expression of the cecropin B-thanatin hybrid antimicrobial peptide in Escherichia coli.
- Author:
Hong-Biao WENG
1
;
Bao-Long NIU
;
Zhi-Qi MENG
;
Meng-Kui XU
Author Information
1. College of Animal Sciences, Zhejiang University, Hangzhou 310029, China. cssswjsz@zaas.org
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Anti-Bacterial Agents;
metabolism;
Antimicrobial Cationic Peptides;
Base Sequence;
Cloning, Molecular;
Escherichia coli;
genetics;
Insect Proteins;
biosynthesis;
Molecular Sequence Data;
Peptides, Cyclic;
biosynthesis;
Recombinant Fusion Proteins;
biosynthesis;
isolation & purification;
pharmacology
- From:
Chinese Journal of Biotechnology
2002;18(3):352-355
- CountryChina
- Language:Chinese
-
Abstract:
A 44-residue hybrid peptide (CB (1-24)-Arg-Ser-Tyr-Tan (4-21)) incorporating 1-24 residues of cecropin B (CB) and 4-21 residues of thanatin (Tan) was designed and constructed. The CB-Tan gene was cloned into expression plasmid pGEX-3X and expressed in E. coli BL21. The fusion protein was purified by affinity chromatography. After digested with enterokinase the gene product released with antibacterial activity and gave one band in Tricine-SDS-PAGE.
