Transforming bivalent ligands into retractable enzyme inhibitors through polypeptide-protein interactions

DOIResolve DOI: http://doi.org/10.1016/j.bmcl.2005.08.085
AuthorSearch for: ; Search for: ; Search for:
TypeArticle
Volume15
Issue23
Pages51205123; # of pages: 4
SubjectEnzyme Inhibitors; Ligands; pha; Protein; Thrombin
AbstractThe concept of bivalent polypeptides with controllable flexible linkers is demonstrated through the design of a new generation of 'antidote'-reversible inhibitors of thrombin. These molecules contain two binding moieties, each of which in isolation has only a moderate affinity of binding, which are linked together by a flexible peptide bridge. We show that activities of the potent bivalent inhibitors of thrombin can be reversed by the specific, but much weaker, binding of the linker moiety to protein 'antidotes'
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47477
NPARC number3538981
Export citationExport as RIS
Report a correctionReport a correction
Record identifier2a5ca9b5-1025-4c74-ba8a-a05425061dfc
Record created2009-03-01
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)