Simple Purification of the Human Antimicrobial Peptide Dermcidin (MDCD-1L) by Intein-Mediated Expression in E-coli
- Authors
- Hong, Inpyo; Kim, Yong-Seok; Choi, Shin-Geon
- Issue Date
- Feb-2010
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Antimicrobial peptides; DCD-1L; dermcidin; intein; protein expression
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.20, no.2, pp.350 - 355
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 20
- Number
- 2
- Start Page
- 350
- End Page
- 355
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/175488
- DOI
- 10.4014/jmb.0907.07029
- ISSN
- 1017-7825
- Abstract
- Among human antimicrobial peptides (hAMPs), DCD-1L has a broad spectrum of antimicrobial activity over a wide pH range and in high salt concentrations. It offers a promising alternative to conventional antibiotics. The 458-bp-long dermcidin cDNA was amplified by PCR using a human fetal cDNA library as a template. The 147-bp fragment of the MDCD-1L gene encoding an additional methionine residue was subcloned into the pTYB11 vector. Recombinant MDCD-1L was expressed as an intein fusion protein in E coli, and then purified by affinity chromatography using chitin beads. A small peptide with a molecular mass of about 5 kDa was detected by tricine gel electrophoresis. The recombinant MDCD-1L peptide was purified from the gel and its amino acid sequence was determined by nanoLC-ESI-MS/MS analysis. The initiating amino acid, methionine, remained attached to the N-terminal region of recombinant MDCD-1L. Purified MDCD-1L showed antimicrobial activity against a Micrococcus luteus test strain.
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