4-Hydroxy-5,6-Dihydro-2H-pyran-2-ones. 3. Bicyclic and hetero-aromatic ring systems as 3-position scaffolds to bind to S1′ and S2′ of the HIV-1 protease enzyme

Autor:	J. V. N. Vara Prasad, Donald Hupe, Elizabeth A. Lunney, John M. Domagala, Donna Ferguson, Greg Zeikus, Neil Graham, Peter J. Tummino, Susan Elizabeth Hagen, Caroline Nouhan, Tod P. Holler, Edmund L. Ellsworth
Rok vydání:	1999
Předmět:	Models Molecular Stereochemistry medicine.medical_treatment Clinical Biochemistry Pharmaceutical Science Hydrocarbons Aromatic Biochemistry Inhibitory Concentration 50 Structure-Activity Relationship chemistry.chemical_compound Sugar Alcohols HIV Protease HIV-1 protease Drug Discovery medicine Structure–activity relationship HIV Protease Inhibitor Computer Simulation Binding site Molecular Biology Binding Sites Protease Molecular Structure biology Bicyclic molecule Organic Chemistry Valine HIV Protease Inhibitors Hydrogen-Ion Concentration chemistry Pyrones Pyran Enzyme inhibitor Drug Design biology.protein Molecular Medicine Software
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 9:2019-2024
ISSN:	0960-894X
Popis:	5,6-Dihydro-2H-pyran-2-ones are potent inhibitors of HIV-1 protease, which bind to the S1, S2, S1', and S2' pockets and have a unique binding mode with the catalytic aspartyl groups and the flap region of the enzyme. Efforts to explore 3-position heterocyclic scaffolds that bind to the S1' and S2' pockets have provided a number of selected analogs that display high HIV-1 protease inhibitory activity. reserved.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d846e90ee22b0fd46c5e28329d3b3d3a https://doi.org/10.1016/s0960-894x(99)00332-7 Zobrazit plný text záznamu Full Text from ScienceDirect