J
Jing Wang
Researcher at Zhejiang University of Technology
Publications - 11
Citations - 615
Jing Wang is an academic researcher from Zhejiang University of Technology. The author has contributed to research in topics: Bovine serum albumin & Binding constant. The author has an hindex of 8, co-authored 8 publications receiving 446 citations.
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Binding interaction of atorvastatin with bovine serum albumin: Spectroscopic methods and molecular docking
TL;DR: The experimental results revealed that the fluorescence quenching mechanism of BSA induced atorvastatin was a combined dynamic and static quench, and the main interaction forces were van der Waals force and hydrogen bonding interaction.
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Binding interaction between sorafenib and calf thymus DNA: spectroscopic methodology, viscosity measurement and molecular docking.
TL;DR: The binding interaction of sorafenib with calf thymus DNA (ct-DNA) was studied using UV-vis absorption spectroscopic, fluorescence emission spectroscopy, circular dichroism (CD), viscosity measurement and molecular docking methods and revealed that there was obvious binding interaction between sorafanib and ct-DNA.
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Binding interaction of sorafenib with bovine serum albumin: Spectroscopic methodologies and molecular docking
TL;DR: The binding interaction of sorafenib with bovine serum albumin (BSA) was studied using fluorescence, circular dichrosim (CD) and molecular docking methods and it could be deduced that sorAFenib was inserted into the subdomain IIA (site I) of BSA and leads to a slight change of the conformation of B SA.
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Characterization of interaction between isoliquiritigenin and bovine serum albumin: Spectroscopic and molecular docking methods
TL;DR: It can be suggested from the molecular docking results that the flexibility ofISL plays an important role in increasing the stability of the whole system upon association of ISL with BSA.
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Intermolecular interaction of prednisolone with bovine serum albumin: Spectroscopic and molecular docking methods
TL;DR: The intermolecular interaction of prednisolone with bovine serum albumin (BSA) was studied using fluorescence, circular dichroism (CD) and molecular docking methods and it could be suggested that the interaction forces were mainly Van der Waals and hydrogen bonding interactions.