ScholarLens Back to search
2014•Advanced materials researchRequires access

High Level Expression and Purification of King Cobra Cathelicidin OH-CATH30 in Escherichia coli as a Thioredoxin Fusion Protein

Tong Yi Sun

Open publisher page 0 citations

Abstract

The Cathelicidin OH-CATH30 may have therapeutic potential against the systemic infections. However, it is a great challenge to obtain abundant OH-CATH30 by Escherichia coli expression system. The OH-CATH30 coding sequence was optimized and subcloned into vector pET-32a, allowing the peptide to be expressed as a thioredoxin fusion protein. The highest protein expression level obtained was 100 mg/L of bacterial culture. Before being cleaved with enterokinase, the released recombinant OH-CATH30 exhibited a in vitro strong antibacterial activity against the control strains.

About this research paper

What this paper is about

The Cathelicidin OH-CATH30 may have therapeutic potential against the systemic infections. However, it is a great challenge to obtain abundant OH-CATH30 by Escherichia coli expression system. The OH-CATH30 coding sequence was optimized and subcloned into vector pET-32a, allowing the peptide to be expressed as a thioredoxin fusion protein. The highest protein expression level obtained was 100 mg/L of bacterial culture. Before being cleaved with enterokinase, the released recombinant OH-CATH30 exhibited a in vitro strong antibacterial activity against the control strains.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

The Cathelicidin OH-CATH30 may have therapeutic potential against the systemic infections. However, it is a great challenge to obtain abundant OH-CATH30 by Escherichia coli expression system. The OH-CATH30 coding sequence was optimized and subcloned into vector pET-32a, allowing the peptide to be expressed as a thioredoxin fusion protein. The highest protein expression level obtained was 100 mg/L of bacterial culture. Before being cleaved with enterokinase, the released recombinant OH-CATH30 exhibited a in vitro strong antibacterial activity against the control strains.

Key concepts: Enteropeptidase, Cathelicidin, Escherichia coli, Thioredoxin, Fusion protein, Recombinant DNA, Molecular biology, Expression vector

Related papers

Related paper 1Related paper 2
Back to paper searchBrowse research topicsOriginal source
High Level Expression and Purification of King Cobra Cathelicidin OH-CATH30 in Escherichia coli as a Thioredoxin Fusion Protein — Research Paper | ScholarLens