Effects of Thioredoxin: SUMO and Intein on Soluble Fusion Expression of an Antimicrobial Peptide OG2 in Escherichia coli
Abstract
OG2 is a modified antimicrobial peptide of Palustrin-OG1 (OG1), which is derived from Odorrana grahami frog. OG2 has shown much higher selective antimicrobial activity and lower hemolytic activity than OG1, indicating OG2 may be a promising antimicrobial agent. In this study, we investigated three fusion partners, including thioredoxin, Mxe GyrA intein, and small ubiquitin-like modifier (SUMO), each fused with OG2, and examined their effects on...
Paper Details
Title
Effects of Thioredoxin: SUMO and Intein on Soluble Fusion Expression of an Antimicrobial Peptide OG2 in Escherichia coli
Published Date
Jan 1, 2013
Journal
Volume
20
Issue
1
Pages
54 - 60
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