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Unraveling the molecular basis for effective regulation of integrin α5ß1 for enhanced therapeutic interventions.
Kumar, Puneet; Sharma, Prerna; Singh, Divya; Mishra, Nidhi; Sarangi, Pranita P.
Afiliación
  • Kumar P; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee, 247667, Uttarakhand, India.
  • Sharma P; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee, 247667, Uttarakhand, India.
  • Singh D; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee, 247667, Uttarakhand, India.
  • Mishra N; Department of Applied Sciences, Indian Institute of Information Technology Allahabad, Prayagraj, 211012, Uttar Pradesh, India.
  • Sarangi PP; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee, 247667, Uttarakhand, India. Electronic address: pranita.sarangi@bt.iitr.ac.in.
Biochem Biophys Res Commun ; 734: 150627, 2024 11 19.
Article en En | MEDLINE | ID: mdl-39236588
ABSTRACT
Cell attachment to the extracellular matrix significantly impacts the integrity of tissues and human health. The integrin α5ß1 is a heterodimer of α5 and ß1 subunits and has been identified as a crucial modulator in several human carcinomas. Integrin α5ß1 significantly regulates cell proliferation, angiogenesis, inflammation, tumor metastasis, and invasion. This regulatory role of integrin α5ß1 in tumor metastasis makes it an appealing target for cancer therapy. The majority of the drugs targeting integrin α5ß1 are limited only to clinical trials. In our study, we have performed 94287 compounds screening to determine potential drugs against α5ß1 integrin. We have used ATN-161 as a reference and employed combined bioinformatic methodologies, including molecular modelling, virtual screening, MM-GBSA, cell-line cytotoxicity prediction, ADMET, Density Functional Theory (DFT), Non-covalent Interactions (NCI) and molecular simulation, to identify putative integrin α5ß1 inhibitors. We found Taxifolin, PD133053, and Acebutolol that possess inhibitory activity against α5ß1 integrin and could act as effective drug for the cancer treatment. Taxifolin, PD133053, and Acebutolol exhibited excellent binding to the druggable pocket of integrin α5ß1, and also maintained a unique binding mechanism with extra hydrophobic contacts at molecular level. Overall, our study gives new pharmacological candidates that may act as a potential drug against integrin α5ß1.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Integrina alfa5beta1 / Antineoplásicos Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2024 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Integrina alfa5beta1 / Antineoplásicos Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2024 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos