|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
20
|
|
pubmed:dateCreated |
2001-2-20
|
|
pubmed:abstractText |
This work describes the use of NMR as a medicinal chemistry tool for better understanding the binding characteristics of inhibitors of the HCV NS3 protease. The protease-bound structure of a tetrapeptide-like inhibitor that has an acid C-terminus, a norvaline at P1 and a naphthylmethoxy proline at P2 is described. Conformational comparisons are made with a similar compound having a 1-amino-cyclopropylcarboxylic acid at P1 and with a hexapeptide inhibitor. Differences between the free and bound states are identified. 19F NMR also helped in determining that a single complex is observed when an inhibitor is added to the protease at a 1:1 ratio.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0960-894X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
16
|
|
pubmed:volume |
10
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2271-4
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
NMR line-broadening and transferred NOESY as a medicinal chemistry tool for studying inhibitors of the hepatitis C virus NS3 protease domain.
|
|
pubmed:affiliation |
Department of Chemistry, Boehringer Ingelheim, Laval, Québec, Canada. slaplante@lav.boehringer-ingelheim.com
|
|
pubmed:publicationType |
Journal Article
|
