Characterization of the interaction between acotiamide hydrochloride and human serum albumin: 1H STD NMR spectroscopy, electrochemical measurement, and docking investigations

RSC Advances ◽  
2016 ◽  
Vol 6 (66) ◽  
pp. 61119-61128 ◽  
Author(s):  
Jiawei He ◽  
Hongqin Yang ◽  
Shanshan Li ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrochemical Measurement ◽  
Binding Mechanism ◽  
Comprehensive Investigation ◽  
Std Nmr

The comprehensive investigation of acotiamide hydrochloride and HSA interaction provides a convictive explanation for its binding mechanism.

scholarly journals Investigating the interaction mechanism of fluorescent whitening agents to human serum albumin using saturation transfer difference-NMR, multi-spectroscopy, and docking studies

RSC Advances ◽  
2017 ◽  
Vol 7 (44) ◽  
pp. 27796-27806 ◽  
Author(s):  
Ludan Zhao ◽  
Jiuyang Liu ◽  
Ronghui Guo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Mechanism ◽  
Docking Studies ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Fluorescent Whitening Agents ◽  
Std Nmr

Characterization of the interaction between two fluorescent whitening agents and human serum albumin: 1H STD-NMR, multi-spectroscopy, and docking studies.

scholarly journals Characterization of the Solution Structure of Human Serum Albumin Loaded with a Metal Porphyrin and Fatty Acids

2011 ◽  
Vol 100 (9) ◽  
pp. 2293-2301 ◽  
Author(s):  
Matthias J.N. Junk ◽  
Hans W. Spiess ◽  
Dariush Hinderberger
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure ◽  
Metal Porphyrin

Highly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor

2020 ◽  
Vol 22 (35) ◽  
pp. 19468-19479 ◽  
Author(s):  
Keiichiro Shiraga ◽  
Mako Urabe ◽  
Takeshi Matsui ◽  
Shojiro Kikuchi ◽  
Yuichi Ogawa
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermal Denaturation ◽  
Hydration Water ◽  
Biological Functions ◽  
Dielectric Sensor ◽  
Hydration State ◽  
Precise Characterization

The biological functions of proteins depend on harmonization with hydration water surrounding them.

Binding mechanism of tauroursodeoxycholic acid to human serum albumin: insights from NMR relaxation and docking simulations

RSC Advances ◽  
2015 ◽  
Vol 5 (15) ◽  
pp. 11036-11042 ◽  
Author(s):  
Di Wu ◽  
Yuanming Zhai ◽  
Jin Yan ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Relaxation ◽  
Binding Mechanism ◽  
Tauroursodeoxycholic Acid ◽  
Docking Simulations ◽  
Relationship Of

Binding patterns and structure–affinity relationship of tauroursodeoxycholic acid with human serum albumin were established by NMR methodology and docking simulations.

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