| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2020483 | Protein Expression and Purification | 2013 | 5 Pages |
•AMP-scolopin 1 was first purified and characterized from the centipede venoms.•We first constructed the expression vector of AMP-scolopin 1.•We first report the application of SUMO fusion technology to the expression and purification of AMP-scolopin 1.•This paper investigated the antimicrobial activity and mechanisms of recombinant scolopin 1.
Antimicrobial peptide scolopin 1 (AMP-scolopin 1) is a small cationic peptide identified from centipede venoms of Scolopendra subspinipes mutilans. It has broad-spectrum activities against bacteria, fungi, and tumor cells, which may possibly be used as an antimicrobial agent. We first report here the application of small ubiquitin-related modifier (SUMO) fusion technology to the expression and purification of cationic antimicrobial peptide AMP-scolopin 1. The fusion protein expressed in a soluble form was purified to a purity of 95% by Ni-IDA chromatography. After the SUMO-scolopin 1 fusion protein was cleaved by the SUMO protease at 30 °C for 1 h, the cleaved sample was reapplied to a Ni-IDA. The recombinant scolopin1 had similar antimicrobial properties to the synthetic scolopin 1. Thus, we successfully established a system for purifying peptide of centipede, which could be used for further research.
