Abstract:
:Beta defensins are antimicrobial peptides (AMPs) with a broad spectrum antimicrobial behavior against pathogens while having minimal tendency to incur pathogen resistance. Human β-defensin 28 (hBD28) is a strongly cationic AMP and hence hypothesized to be highly effective in permeabilizing negatively-charged pathogen membranes. However, the scarcity of hBD28 in vivo has impeded detailed structure and antimicrobial studies of hBD28. Chemical synthesis of hBD28 rendered extremely poor yields due to inefficient cysteine oxidation. In this study, a rapid and scalable production route to produce bioactive hBD28 in Escherichia coli (E. coli) is reported. The design of a dual fusion tag expression construct was pivotal in enhancing soluble expression and easing purification of hBD28. The final hBD28 (purity >95%) displayed significant antimicrobial activity against E. coli K12 and showed dose-dependent killing kinetics. Circular dichroism spectroscopy confirmed the presence of both β-sheet and α-helix conformations in the secondary structure of hBD28.
journal_name
Biotechnol Bioengjournal_title
Biotechnology and bioengineeringauthors
Tay DK,Rajagopalan G,Li X,Chen Y,Lua LH,Leong SSdoi
10.1002/bit.22970subject
Has Abstractpub_date
2011-03-01 00:00:00pages
572-81issue
3eissn
0006-3592issn
1097-0290journal_volume
108pub_type
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