198904-86-8Relevant articles and documents
NOVEL AZA-PEPTIDES CONTAINING 2,2-DISUBSTITUTED CYCLOBUTYL AND/OR SUBSTITUTED ALKOXY BENZYL DERIVATIVES AS ANTIVIRALS
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Page/Page column 33, (2011/07/30)
The present invention relates to novel aza-peptides containing 2,2-disubstituted 5 cyclobutyl and/or substituted alkoxy benzyl derivatives of formula (I) and compositions for inhibiting Human Immunodeficiency Virus (HIV) and process for making the compounds.
A rare pyridine to pyrrole conversion leading to a side product in epoxide ring opening
Pathirana, Charles,Shukla, Rajesh,Castoro, John,Weaver, Douglas,Byrne, Liam,Pennarun-Thomas, Gaelle,Palaniswamy, Venkatapuram
scheme or table, p. 1586 - 1587 (2009/06/28)
A minor side product in a manufacturing batch of the intermediate 4 was observed and separated. The minor side product 5 was purified by preparative HPLC and its structure was determined by the analysis of comprehensive NMR and MS data. The structure of 5
Design and synthesis of HIV-1 protease inhibitors incorporating oxazolidinones as P2/P2′ ligands in pseudosymmetric dipeptide isosteres
Reddy, G. S. Kiran Kumar,Ali, Akbar,Nalam, Madhavi N. L.,Anjum, Saima Ghafoor,Cao, Hong,Nathans, Robin S.,Schiffer, Celia A.,Rana, Tariq M.
, p. 4316 - 4328 (2008/02/12)
A series of novel HIV-1 protease inhibitors based on two pseudosymmetric dipeptide isosteres have been synthesized and evaluated. The inhibitors were designed by incorporating N-phenyloxazolidinone-5-carboxamides into the hydroxyethylene and (hydroxyethyl)hydrazine dipeptide isosteres as P2 and P2′ ligands. Compounds with (S)-phenyloxazolidinones attached at a position proximal to the central hydroxyl group showed low nM inhibitory activities against wild-type HIV-1 protease. Selected compounds were further evaluated for their inhibitory activities against a panel of multidrug-resistant protease variants and for their antiviral potencies in MT-4 cells. The crystal structures of lopinavir (LPV) and two new inhibitors containing phenyloxazolidinone-based ligands in complex with wild-type HIV-1 protease have been determined. A comparison of the inhibitor-protease structures with the LPV-protease structure provides valuable insight into the binding mode of the new inhibitors to the protease enzyme. Based on the crystal structures and knowledge of structure-activity relationships, new inhibitors can be designed with enhanced enzyme inhibitory and antiviral potencies.