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

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.

RSC Advances ◽  
2015 ◽  
Vol 5 (96) ◽  
pp. 79107-79118 ◽  
Author(s):  
Somnath Dasmandal ◽  
Arjama Kundu ◽  
Suparna Rudra ◽  
Ambikesh Mahapatra

Exploration of binding interaction between anionic amino acid surfactant and BSA.


2014 ◽  
Vol 49 (4) ◽  
pp. 623-630 ◽  
Author(s):  
Muzaffar Ul Hassan Mir ◽  
Jitendra Kumar Maurya ◽  
Shahnawaz Ali ◽  
Shah Ubaid-ullah ◽  
Abbul Bashar Khan ◽  
...  

2019 ◽  
Vol 2019 ◽  
pp. 1-12 ◽  
Author(s):  
Abdulrahman A. Al-Mehizia ◽  
Ahmed H. Bakheit ◽  
Seema Zargar ◽  
Mashooq A. Bhat ◽  
Majid Mohammed Asmari ◽  
...  

In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (5d) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug 5d was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the 5d and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and 5d interaction was static quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and 5d interaction. The Förster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-5d interaction. This binding interaction study provided a basis to comprehend the binding interaction between 5d and BSA. These results provided information about sites of BSA involved in its interaction with 5d.


2021 ◽  
Author(s):  
Jonathan Osiris Vicente-Escobar ◽  
Miguel A. García-Sánchez ◽  
F. González ◽  
S. Cipagauta-Díaz ◽  
A. Estrella González

RSC Advances ◽  
2018 ◽  
Vol 8 (13) ◽  
pp. 7280-7286 ◽  
Author(s):  
Jianli Liu ◽  
Yonglin He ◽  
Dan Liu ◽  
Yin He ◽  
Zhipeng Tang ◽  
...  

The interaction of astilbin with bovine serum albumin was confirmed by multi-spectroscopic techniques and molecular docking methods.


2019 ◽  
Vol 22 ◽  
pp. 100254 ◽  
Author(s):  
Shilpa R. Patil ◽  
Sonali M. Salunkhe ◽  
Saubai B. Wakshe ◽  
Kshipra S. Karnik ◽  
Aniket P. Sarkate ◽  
...  

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