Study of the structure-activity relationship of flavonoids based on their interaction with human serum albumin

RSC Advances ◽  
2015 ◽  
Vol 5 (89) ◽  
pp. 73290-73300 ◽  
Author(s):  
Bao Tu ◽  
Zhi-Feng Chen ◽  
Zhi-Juan Liu ◽  
Rong-Rong Li ◽  
Yu Ouyang ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Functional Groups ◽  
Conformation Change ◽  
Multiple Methods ◽  
Structure Activity ◽  
Relationship Of

The influence of functional groups on the interaction has been studied detailed here; fluorescence quenching degrees and the conformation change are considered through multiple methods; molecular docking has been introduced to verify related results.

scholarly journals Molecular Structure-Affinity Relationship of Bufadienolides and Human Serum Albumin In Vitro and Molecular Docking Analysis

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0126669 ◽  
Author(s):  
Jing Zhou ◽  
Guodi Lu ◽  
Honglan Wang ◽  
Junfeng Zhang ◽  
Jinao Duan ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Analysis ◽  
Relationship Of ◽  
Molecular Docking Analysis

scholarly journals Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches

RSC Advances ◽  
2019 ◽  
Vol 9 (55) ◽  
pp. 31969-31978 ◽  
Author(s):  
Priyanka Yadav ◽  
Jitendra Kumar Yadav ◽  
Alka Agarwal ◽  
Satish K. Awasthi
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Studies ◽  
Visible Absorption ◽  
Molecular Docking Studies ◽  
Uv Visible ◽  
Circular Dichroïsm

Mechanistic insights into the interaction of five previously chemically synthesized triazole-linked chalcone analogs with human serum albumin were analyzed using UV-visible absorption, fluorescence quenching, circular dichroism and molecular docking studies.

scholarly journals Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and In Silico Approaches

2019 ◽  
Vol 20 (3) ◽  
pp. 662 ◽  
Author(s):  
Mohammad Baig ◽  
Safikur Rahman ◽  
Gulam Rabbani ◽  
Mohd Imran ◽  
Khurshid Ahmad ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Docking ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Muscle Relaxant ◽  
In Silico ◽  
Dynamics Simulation ◽  
Insight Into

Cyclobenzaprine hydrochloride (CBH) is a well-known muscle relaxant that is widely used to relieve muscle spasms and other pain associated with acute musculoskeletal conditions. In this study, we elucidated the binding characteristics of this muscle relaxant to human serum albumin (HSA). From a pharmaceutical and biochemical viewpoint, insight into the structure, functions, dynamics, and features of HSA-CBH complex holds great importance. The binding of CBH with this major circulatory transport protein was studied using a combination of biophysical approaches such as UV-VIS absorption, fluorescence quenching, and circular dichroism (CD) spectroscopy. Various in silico techniques, molecular docking and molecular dynamics, were also used to gain deeper insight into the binding. A reduction in the fluorescence intensities of HSA-CBH complex with a constant increase in temperature, revealed the static mode of protein fluorescence quenching upon CBH addition, which confirmed the formation of the HSA-CBH ground state complex. The alteration in the UV-VIS and far-UV CD spectrum indicated changes in both secondary and tertiary structures of HSA upon binding of CBH, further proving CBH binding to HSA. The analysis of thermodynamic parameters ∆H° and ∆S° showed that binding of CBH to HSA was dominated by intermolecular hydrophobic forces. The results of the molecular docking and molecular dynamics simulation studies also confirmed the stability of the complex and supported the experimental results.

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