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Production of human antimicrobial peptide LL-37 in Escherichia coli using a thioredoxin-SUMO dual fusion system
被引:26
|作者:
Li, Yifeng
[1
]
机构:
[1] Univ Texas Hlth Sci Ctr San Antonio, Dept Biochem, Prot Prod Core Facil, San Antonio, TX 78229 USA
关键词:
Antimicrobial peptide;
Dual-tag;
Fusion protein;
LL-37;
SUMO;
Thioredoxin;
CATHELICIDIN LL-37;
RECOMBINANT PRODUCTION;
EXPRESSION;
PURIFICATION;
FAMILY;
ROLES;
D O I:
10.1016/j.pep.2012.10.008
中图分类号:
Q5 [生物化学];
学科分类号:
071010 ;
081704 ;
摘要:
LL-37 is a human antimicrobial peptide that has been shown to possess multiple functions in host defense. In this report, the peptide was expressed as a fusion with a thioredoxin SUMO dual-tag. Upon SUMO protease mediated cleavage at the SUMO/peptide junction, LL-37 with its native N-terminus was generated. The released peptide was separated from the dual-tag and cleavage enzyme by size-exclusion chromatography. Mass spectrometry analysis proves that the recombinant peptide has a molecular weight as theoretically expected for its native form. The produced peptide displayed antimicrobial activity against Escherichia coli K-12. On average, 2.4 mg peptide was obtained from one liter of bacterial culture. Thus, the described approach provides an effective alternative for producing active recombinant LL-37 with its natural amino acid sequence in E. coli. (C) 2012 Elsevier Inc. All rights reserved.
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页码:72 / 78
页数:7
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