Analysis of binding interaction between pegylated puerarin and bovine serum albumin by spectroscopic methods and dynamic light scattering

2011 ◽  
Vol 83 (1) ◽  
pp. 453-460 ◽  
Author(s):  
Meirong Yu ◽  
Zhishan Ding ◽  
Fusheng Jiang ◽  
Xinghong Ding ◽  
Jinyue Sun ◽  
...  
Keyword(s):  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Dynamic Light Scattering ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Methods ◽  
Binding Interaction

scholarly journals Binding studies of paeonolum with bovine serum albumin using spectroscopic methods

2007 ◽  
Vol 21 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Chang-yun Chen ◽  
Xiao-tian Gu ◽  
Jia-hong Zhou
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Interaction Process ◽  
Spectroscopic Methods ◽  
Spectroscopic Techniques ◽  
Bioactive Components ◽  
Binding Studies ◽  
Binding Interaction ◽  
Physiological Conditions

Fluorescence and UV spectroscopic techniques were used to investigate the interaction of Paeonolum, one of the major bioactive components isolated from the bark of peony plant, with bovine serum albumin (BSA). Results obtained reveal that a binding interaction occurs between paeonolum and BSA under physiological conditions, and the interaction can quench the fluorescence of BSA originating from the complex formation between paeonolum and BSA. In addition, according to the thermodynamics parameters of this interaction process, it appears that this binding interaction is mainly hydrophobic in nature.

Exploring the thermodynamics and conformational aspects of nicotinic acid binding with bovine serum albumin: a detailed calorimetric, spectroscopic and molecular docking study

RSC Advances ◽  
2016 ◽  
Vol 6 (41) ◽  
pp. 34754-34769 ◽  
Author(s):  
Tarlok Singh Banipal ◽  
Amandeep Kaur ◽  
Imran Ahmd Khan ◽  
Parampaul Kaur Banipal
Keyword(s):  
Molecular Docking ◽  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Docking Study ◽  
Vitamin B ◽  
Spectroscopic Techniques ◽  
Molecular Docking Study ◽  
Binding Interaction

An attempt to obtain a physicochemical and conformational outlook on the binding interaction of vitamin B3 (NA) with a model transport protein BSA using calorimetry, light scattering, molecular docking, and spectroscopic techniques.

Buffers more than buffering agent: introducing a new class of stabilizers for the protein BSA

2015 ◽  
Vol 17 (2) ◽  
pp. 1114-1133 ◽  
Author(s):  
Bhupender S. Gupta ◽  
Mohamed Taha ◽  
Ming-Jer Lee
Keyword(s):  
Thermal Stability ◽  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Dynamic Light Scattering ◽  
Serum Albumin ◽  
Bovine Serum ◽  
New Class ◽  
Buffering Agent ◽  
Thermal Stability Of ◽  
Biological Buffers

In this study, we have analyzed the influence of four biological buffers on the thermal stability of bovine serum albumin (BSA) using dynamic light scattering (DLS).

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