Journal
PROTEIN AND PEPTIDE LETTERS
Volume 16, Issue 6, Pages 668-676Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986609788490122
Keywords
HBD2; Defensin; Peptide; E. coli; Chemotaxis; Antimicrobial activity
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC)
- Engineering and Physical Sciences Research Council (EPSRC)
- Cystic Fibrosis Trust
- University of Edinburgh
- Medical Research Council UK (MRC)
- Scottish Enterprise and the Royal Society of Edinburgh
- MRC [MC_U127527201] Funding Source: UKRI
- Medical Research Council [MC_U127527201] Funding Source: researchfish
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Human beta-defensin 2 (HBD2) has been shown to interact with pathogenic bacteria and components of the mammalian innate and adaptive immune response. We describe a quick and reliable method for the production of HBD2 in Escherichia coli. HBD2 was expressed as an insoluble fusion, chemically cleaved and oxidised to give a single, folded HBD2 beta-isoform. The purified peptide was analysed by high resolution mass spectrometry, displayed a well-dispersed H-1 NMR spectrum, was a chemoattractant to HEK293 cells expressing CCR6 and acted as an antimicrobial agent against E. coli, P. aeruginosa, C. albicans and S. aureus.
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