التفاصيل البيبلوغرافية
| العنوان: |
Target specificity of selective bioactive compounds in blocking a-dystroglycan receptor to suppress Lassa virus infection: an in silico approach. |
| المؤلفون: |
Arefin, Adittya, Ema, Tanzila Ismail, Islam, Tamnia, Hossen, Md. Saddam, Islam, Tariqul, Azad, Salauddin Al, Badal, Md. Nasir Uddin, Islam, Md. Aminul, Biswas, Partha, Alam, Nafee Ul, Islam, Enayetul, Anjum, Maliha, Masud, Afsana, Kamran, Md. Shaikh, Rahman, Ahsab, Paul, Parag Kumar |
| المصدر: |
Journal of Biomedical Research; Nov2021, Vol. 35 Issue 6, p459-473, 15p |
| مصطلحات موضوعية: |
BIOACTIVE compounds, VIRUS diseases, AMINO acid residues, MOLECULAR dynamics, STRUCTURE-activity relationships |
| مستخلص: |
Lassa hemorrhagic fever, caused by Lassa mammarenavirus (LASV) infection, accumulates up to 5000 deaths every year. Currently, there is no vaccine available to combat this disease. In this study, a library of 200 bioactive compounds was virtually screened to study their drug-likeness with the capacity to block the α-dystroglycan (α- DG) receptor and prevent LASV influx. Following rigorous absorption, distribution, metabolism, and excretion (ADME) and quantitative structure-activity relationship (QSAR) profiling, molecular docking was conducted with the top ligands against the α-DG receptor. The compounds chrysin, reticuline, and 3-caffeoylshikimic acid emerged as the top three ligands in terms of binding affinity. Post-docking analysis revealed that interactions with Arg76, Asn224, Ser259, and Lys302 amino acid residues of the receptor protein were important for the optimum binding affinity of ligands. Molecular dynamics simulation was performed comprehensively to study the stability of the protein-ligand complexes. In-depth assessment of root-mean-square deviation (RMSD), root mean square fluctuation (RMSF), polar surface area (PSA), B-Factor, radius of gyration (Rg), solvent accessible surface area (SASA), and molecular surface area (MolSA) values of the protein-ligand complexes affirmed that the candidates with the best binding affinity formed the most stable protein-ligand complexes. To authenticate the potentialities of the ligands as target-specific drugs, an in vivo study is underway in real time as the continuation of the research. [ABSTRACT FROM AUTHOR] |
|
Copyright of Journal of Biomedical Research is the property of Journal of Nanjing Medicial University (NMU) Medical Publications Center and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
