mvt-101 and Acquired-Immunodeficiency-Syndrome

mvt-101 has been researched along with Acquired-Immunodeficiency-Syndrome* in 1 studies

Other Studies

1 other study(ies) available for mvt-101 and Acquired-Immunodeficiency-Syndrome

Article	Year
A novel nonpeptide HIV-1 protease inhibitor: elucidation of the binding mode and its application in the design of related analogs. Journal of medicinal chemistry, 1994, Aug-19, Volume: 37, Issue:17 HIV-1 protease has been identified as a significant target enzyme in AIDS research. While numerous peptide-derived inhibitors have been described, the identification of a nonpeptide inhibitor remains an important goal. Using an HIV-1 protease mass screening technique, 4-hydroxy-3-(3-phenoxypropyl)-2H-1-benzopyran-2-one (1) was identified as a nonpeptide competitive inhibitor of the enzyme. Employing a Monte Carlo-based docking procedure, the coumarin was docked in the active site of the enzyme, revealing a binding mode that was later confirmed by the X-ray crystal analysis. Several analogs were prepared to test the binding interactions and improve the overall binding affinity. The most active compound in the study was 4,7-dihydroxy-3-[4-(2-methoxyphenyl)butyl]-2H-1-benzopyran-2-one (31). Topics: 4-Hydroxycoumarins; Acquired Immunodeficiency Syndrome; Binding Sites; Coumarins; Crystallography, X-Ray; Drug Design; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Models, Molecular; Molecular Conformation; Molecular Structure; Monte Carlo Method; Oligopeptides; Protein Conformation	1994

Article

Year

A novel nonpeptide HIV-1 protease inhibitor: elucidation of the binding mode and its application in the design of related analogs.

Journal of medicinal chemistry, 1994, Aug-19, Volume: 37, Issue:17

HIV-1 protease has been identified as a significant target enzyme in AIDS research. While numerous peptide-derived inhibitors have been described, the identification of a nonpeptide inhibitor remains an important goal. Using an HIV-1 protease mass screening technique, 4-hydroxy-3-(3-phenoxypropyl)-2H-1-benzopyran-2-one (1) was identified as a nonpeptide competitive inhibitor of the enzyme. Employing a Monte Carlo-based docking procedure, the coumarin was docked in the active site of the enzyme, revealing a binding mode that was later confirmed by the X-ray crystal analysis. Several analogs were prepared to test the binding interactions and improve the overall binding affinity. The most active compound in the study was 4,7-dihydroxy-3-[4-(2-methoxyphenyl)butyl]-2H-1-benzopyran-2-one (31).

Topics: 4-Hydroxycoumarins; Acquired Immunodeficiency Syndrome; Binding Sites; Coumarins; Crystallography, X-Ray; Drug Design; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Models, Molecular; Molecular Conformation; Molecular Structure; Monte Carlo Method; Oligopeptides; Protein Conformation

1994