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@article{Dang:2012:10.1016/j.bmc.2011.06.042,
author = {Dang, THT and Fagan, RP and Fairweather, NF and Tate, EW},
doi = {10.1016/j.bmc.2011.06.042},
journal = {Bioorganic & Medicinal Chemistry},
pages = {614--621},
title = {Novel inhibitors of surface layer processing in Clostridium difficile},
url = {http://dx.doi.org/10.1016/j.bmc.2011.06.042},
volume = {20},
year = {2012}
}
TY - JOUR
AB - Clostridium difficile, a leading cause of hospital-acquired bacterial infection, is coated in a dense surface layer (S-layer) that is thought to provide both physicochemical protection and a scaffold for host-pathogen interactions. The key structural components of the S-layer are two proteins derived from a polypeptide precursor, SlpA, via proteolytic cleavage by the protease Cwp84. Here, we report the design, synthesis and in vivo characterization of a panel of protease inhibitors and activity-based probes (ABPs) designed to target S-layer processing in live C. difficile cells. Inhibitors based on substrate-mimetic peptides bearing a C-terminal Michael acceptor warhead were found to be promising candidates for further development.
AU - Dang,THT
AU - Fagan,RP
AU - Fairweather,NF
AU - Tate,EW
DO - 10.1016/j.bmc.2011.06.042
EP - 621
PY - 2012///
SN - 1464-3391
SP - 614
TI - Novel inhibitors of surface layer processing in Clostridium difficile
T2 - Bioorganic & Medicinal Chemistry
UR - http://dx.doi.org/10.1016/j.bmc.2011.06.042
UR - http://hdl.handle.net/10044/1/26863
VL - 20
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821