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Virtual Screening for Potential Phytobioactives as Therapeutic Leads to Inhibit NQO1 for Selective Anticancer Therapy.
Shreevatsa, Bhargav; Dharmashekara, Chandan; Swamy, Vikas Halasumane; Gowda, Meghana V; Achar, Raghu Ram; Kameshwar, Vivek Hamse; Thimmulappa, Rajesh Kumar; Syed, Asad; Elgorban, Abdallah M; Al-Rejaie, Salim S; Ortega-Castro, Joaquín; Frau, Juan; Flores-Holguín, Norma; Shivamallu, Chandan; Kollur, Shiva Prasad; Glossman-Mitnik, Daniel.
Afiliación
  • Shreevatsa B; Department of Biotechnology and Bioinformatics, School of Life Sciences, JSS Academy of Higher Education and Research, Mysuru 570015, India.
  • Dharmashekara C; Department of Biotechnology and Bioinformatics, School of Life Sciences, JSS Academy of Higher Education and Research, Mysuru 570015, India.
  • Swamy VH; Division of Biochemistry, School of Life Sciences, JSS Academy of Higher Education and Research, Mysuru 570015, India.
  • Gowda MV; Division of Biochemistry, School of Life Sciences, JSS Academy of Higher Education and Research, Mysuru 570015, India.
  • Achar RR; Division of Biochemistry, School of Life Sciences, JSS Academy of Higher Education and Research, Mysuru 570015, India.
  • Kameshwar VH; School of Natural Science, Adichunchanagiri University, B.G. Nagara, Nagamangala, Mandya 571448, India.
  • Thimmulappa RK; Department of Biochemistry, JSS Medical College, JSS Academy of Higher Education and Research, Mysuru 570015, India.
  • Syed A; Department of Botany and Microbiology, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia.
  • Elgorban AM; Department of Botany and Microbiology, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia.
  • Al-Rejaie SS; Department of Pharmacology and Toxicology, College of Pharmacy, King Saud University, P.O. Box 55760, Riyadh 11451, Saudi Arabia.
  • Ortega-Castro J; Departament de Química, Universitat de les Illes Balears, 07122 Palma de Malllorca, Spain.
  • Frau J; Departament de Química, Universitat de les Illes Balears, 07122 Palma de Malllorca, Spain.
  • Flores-Holguín N; Laboratorio Virtual NANOCOSMOS, Departamento de Medio Ambiente y Energía, Centro de Investigación en Materiales Avanzados, Chihuahua 31136, Mexico.
  • Shivamallu C; Department of Biotechnology and Bioinformatics, School of Life Sciences, JSS Academy of Higher Education and Research, Mysuru 570015, India.
  • Kollur SP; Department of Sciences, Mysuru Campus, Amrita School of Arts and Sciences, Amrita Vishwa Vidyapeetham, Mysuru 570026, India.
  • Glossman-Mitnik D; Laboratorio Virtual NANOCOSMOS, Departamento de Medio Ambiente y Energía, Centro de Investigación en Materiales Avanzados, Chihuahua 31136, Mexico.
Molecules ; 26(22)2021 Nov 14.
Article en En | MEDLINE | ID: mdl-34833955
NAD(P)H:quinone acceptor oxidoreductase-1 (NQO1) is a ubiquitous flavin adenine dinucleotide-dependent flavoprotein that promotes obligatory two-electron reductions of quinones, quinonimines, nitroaromatics, and azo dyes. NQO1 is a multifunctional antioxidant enzyme whose expression and deletion are linked to reduced and increased oxidative stress susceptibilities. NQO1 acts as both a tumor suppressor and tumor promoter; thus, the inhibition of NQO1 results in less tumor burden. In addition, the high expression of NQO1 is associated with a shorter survival time of cancer patients. Inhibiting NQO1 also enables certain anticancer agents to evade the detoxification process. In this study, a series of phytobioactives were screened based on their chemical classes such as coumarins, flavonoids, and triterpenoids for their action on NQO1. The in silico evaluations were conducted using PyRx virtual screening tools, where the flavone compound, Orientin showed a better binding affinity score of -8.18 when compared with standard inhibitor Dicumarol with favorable ADME properties. An MD simulation study found that the Orientin binding to NQO1 away from the substrate-binding site induces a potential conformational change in the substrate-binding site, thereby inhibiting substrate accessibility towards the FAD-binding domain. Furthermore, with this computational approach we are offering a scope for validation of the new therapeutic components for their in vitro and in vivo efficacy against NQO1.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: NAD(P)H Deshidrogenasa (Quinona) / Fitoquímicos / Neoplasias / Antineoplásicos Tipo de estudio: Diagnostic_studies / Screening_studies Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2021 Tipo del documento: Article País de afiliación: India

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: NAD(P)H Deshidrogenasa (Quinona) / Fitoquímicos / Neoplasias / Antineoplásicos Tipo de estudio: Diagnostic_studies / Screening_studies Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2021 Tipo del documento: Article País de afiliación: India