Abstract
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.
Original language | English |
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Pages (from-to) | 668-676 |
Number of pages | 9 |
Journal | Protein and Peptide Letters |
Volume | 16 |
Issue number | 6 |
DOIs | |
Publication status | Published - Jun 2009 |