| Literature DB >> 26000468 |
Maren Kuhnert1, Andreas Blum1, Holger Steuber2, Wibke E Diederich1.
Abstract
3,4-disubstituted pyrrolidines originally designed to inhibit the closely related HIV-1 protease were evaluated as privileged structures against HTLV-1 protease (HTLV-1 PR). The most potent inhibitor of this series exhibits two-digit nanomolar affinity and represents, to the best of our knowledge, the most potent nonpeptidic inhibitor of HTLV-1 PR described so far. The X-ray structures of two representatives bound to HTLV-1 PR were determined, and the structural basis of their affinity is discussed.Entities:
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Year: 2015 PMID: 26000468 DOI: 10.1021/acs.jmedchem.5b00346
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446