Pub. Date : 2022
PMID : 35498163
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Objective: To study structure-specific solubilization effect of Sulfobutyl ether-beta-cyclodextrin (SBE-beta-CD) on Remdesivir (RDV) and to understand the experimental clathration with the aid of quantum mechanics (QM), molecular docking and molecular dynamics (MD) calculations. | remdesivir | ACD shelterin complex subunit and telomerase recruitment factor | Homo sapiens |
| 2 | Objective: To study structure-specific solubilization effect of Sulfobutyl ether-beta-cyclodextrin (SBE-beta-CD) on Remdesivir (RDV) and to understand the experimental clathration with the aid of quantum mechanics (QM), molecular docking and molecular dynamics (MD) calculations. | remdesivir | ACD shelterin complex subunit and telomerase recruitment factor | Homo sapiens |
| 3 | Results: The phase solubility and solubilization effect of RDV in SBE-beta-CD were explored kinetically and thermodynamically for each assessed condition. | remdesivir | ACD shelterin complex subunit and telomerase recruitment factor | Homo sapiens |
| 4 | An optimal drug / SBE-beta-CD feeding molar ratio was determined stoichiometrically for RDV solubility in pH1.7 solution. | remdesivir | ACD shelterin complex subunit and telomerase recruitment factor | Homo sapiens |
| 5 | A possible hypothesis was raised to elucidate the experimentally observed stabilization of supersaturation based on the proposed RDV Cation A /SBE-beta-CD pocket conformations. | remdesivir | ACD shelterin complex subunit and telomerase recruitment factor | Homo sapiens |
| 6 | Conclusion: The computational explorations conformed to the experimentally determined phase solubilization and well elucidated the mechanism of macroscopic clathration between RDV and SBE-beta-CD from the perspective of microscopic molecular calculations. | remdesivir | ACD shelterin complex subunit and telomerase recruitment factor | Homo sapiens |