Structural highlights
Publication Abstract from PubMed
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.
Privileged Structures Meet Human T-Cell Leukemia Virus-1 (HTLV-1): C2-Symmetric 3,4-Disubstituted Pyrrolidines as Nonpeptidic HTLV-1 Protease Inhibitors.,Kuhnert M, Blum A, Steuber H, Diederich WE J Med Chem. 2015 Jun 11;58(11):4845-50. doi: 10.1021/acs.jmedchem.5b00346. Epub, 2015 May 22. PMID:26000468[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuhnert M, Blum A, Steuber H, Diederich WE. Privileged Structures Meet Human T-Cell Leukemia Virus-1 (HTLV-1): C2-Symmetric 3,4-Disubstituted Pyrrolidines as Nonpeptidic HTLV-1 Protease Inhibitors. J Med Chem. 2015 Jun 11;58(11):4845-50. doi: 10.1021/acs.jmedchem.5b00346. Epub, 2015 May 22. PMID:26000468 doi:http://dx.doi.org/10.1021/acs.jmedchem.5b00346
