In this section
@article{Roqué:2014:10.1016/j.bmcl.2013.12.045,
author = {Roqué, Rosell NR and Mokhlesi, L and Milton, NE and Sweeney, TR and Zunszain, PA and Curry, S and Leatherbarrow, RJ},
doi = {10.1016/j.bmcl.2013.12.045},
journal = {Bioorg Med Chem Lett},
pages = {490--494},
title = {Design and synthesis of irreversible inhibitors of foot-and-mouth disease virus 3C protease.},
url = {http://dx.doi.org/10.1016/j.bmcl.2013.12.045},
volume = {24},
year = {2014}
}
TY - JOUR
AB - Foot-and-mouth disease virus (FMDV) causes a highly infectious and economically devastating disease of livestock. The FMDV genome is translated as a single polypeptide precursor that is cleaved into functional proteins predominantly by the highly conserved viral 3C protease, making this enzyme an attractive target for antiviral drugs. A peptide corresponding to an optimal substrate has been modified at the C-terminus, by the addition of a warhead, to produce irreversible inhibitors that react as Michael acceptors with the enzyme active site. Further investigation highlighted key structural determinants for inhibition, with a positively charged P2 being particularly important for potency.
AU - Roqué,Rosell NR
AU - Mokhlesi,L
AU - Milton,NE
AU - Sweeney,TR
AU - Zunszain,PA
AU - Curry,S
AU - Leatherbarrow,RJ
DO - 10.1016/j.bmcl.2013.12.045
EP - 494
PY - 2014///
SP - 490
TI - Design and synthesis of irreversible inhibitors of foot-and-mouth disease virus 3C protease.
T2 - Bioorg Med Chem Lett
UR - http://dx.doi.org/10.1016/j.bmcl.2013.12.045
UR - http://www.ncbi.nlm.nih.gov/pubmed/24374278
UR - http://hdl.handle.net/10044/1/12642
VL - 24
ER -
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