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Identification of potential inhibitors targeting Ebola virus VP35 protein: a computational strategy.
Chen, Yan-Kun; Gahtani, Reem M; Al Shahrani, Mesfer; Hani, Umme; Alshabrmi, Fahad M; Alam, Sarfaraz; Almohaimeed, Hailah M; Basabrain, Ammar A; Shahab, Muhammad; Xie, Meng-Zhou.
Afiliación
  • Chen YK; School of Chinese Medicine, Hunan University of Chinese Medicine, Changsha, China.
  • Gahtani RM; Precision Medicine R&D Center, Zhuhai Institute of Advanced Technology, Zhuhai, China.
  • Al Shahrani M; Department of Clinical Laboratory Sciences, College of Applied Medical Sciences, King Khalid University, Abha, Saudi Arabia.
  • Hani U; Department of Clinical Laboratory Sciences, College of Applied Medical Sciences, King Khalid University, Abha, Saudi Arabia.
  • Alshabrmi FM; Department of Pharmaceutics, College of Pharmacy, King Khalid University, Abha,Saudia Arabia.
  • Alam S; Department of Medical Laboratories, College of Applied Medical Sciences, Qassim University, Saudi Arabia.
  • Almohaimeed HM; Tunneling Group, Biotechnology Centre, Silesian University of Technology, Gliwice, Poland.
  • Basabrain AA; Department of Basic Science, College of Medicine, Princess Nourah bint Abdulrahman University, Riyadh, Saudi Arabia.
  • Shahab M; Department of Medical Laboratory Sciences, Faculty of Applied Medical Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
  • Xie MZ; Hematology Research Unit, King Fahd Medical Research Center, King Abdulaziz University, Jeddah, Saudi Arabia.
J Biomol Struct Dyn ; : 1-13, 2023 Dec 20.
Article en En | MEDLINE | ID: mdl-38124513
ABSTRACT
Ebola virus (EBOV) poses a severe threat as a highly infectious pathogen, causing devastating hemorrhagic fever in both humans and animals. The EBOV virus VP35 protein plays a crucial role in viral replication and exhibits the ability to suppress the host interferon cascade, leading to immune system depletion. As a potential drug target, VP35 protein inhibition holds promise for combating EBOV. To discover new drug candidates, we employed a computer-aided drug design approach, focusing on compounds capable of inhibiting VP35 protein replication. In this connection, a pharmacophore model was generated using molecular interactions between the VP35 protein and its inhibitor. ZINC and Cambridge database were screened using validated pharmacophore model. Further the compounds were filtered based on Lipinski's rule of five and subjected to MD simulation and relative binding free energy calculation. Six compounds manifest a significant docking score and strong binding interaction towards VP35 protein. MD simulations further confirmed the remarkable stability of these six complexes. Relative binding free energy calculations also showed significant ΔG value in the range of -132.3 and -49.3 kcal/mol. This study paves the way for further optimization of these compounds as potential inhibitors of VP35, facilitating subsequent experimental in vitro studies.Communicated by Ramaswamy H. Sarma.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Biomol Struct Dyn Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Biomol Struct Dyn Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido