Molecular level insight into the effect of triethyloctylammonium bromide on the structure, thermal stability, and activity of Bovine serum albumin

2018 ◽  
Vol 107 ◽  
pp. 186-193 ◽  
Author(s):  
Lakkoji Satish ◽  
Sabera Millan ◽  
Visakh Vijayalekshmi Sasidharan ◽  
Harekrushna Sahoo
2017 ◽  
Vol 46 (4) ◽  
pp. 831-848 ◽  
Author(s):  
Lakkoji Satish ◽  
Sabera Millan ◽  
Satyabrata Das ◽  
Sarita Jena ◽  
Harekrushna Sahoo

2014 ◽  
Vol 27 (5) ◽  
pp. 239-249 ◽  
Author(s):  
Yan Liu ◽  
Mingmao Chen ◽  
Shuaihua Wang ◽  
Jingjing Lin ◽  
Lizhen Cai ◽  
...  

2017 ◽  
Vol 176 ◽  
pp. 75-82 ◽  
Author(s):  
Guo Li ◽  
Jianying Huang ◽  
Tao Chen ◽  
Xiangyang Wang ◽  
Haijiang Zhang ◽  
...  

2020 ◽  
Vol 154 ◽  
pp. 1448-1459 ◽  
Author(s):  
Tajalli Ilm Chandel ◽  
Mariyam Afghani ◽  
Aiman Masroor ◽  
Ibrar Ahmad Siddique ◽  
Syed Mohammad Zakariya ◽  
...  

2020 ◽  
Vol 22 (42) ◽  
pp. 24410-24422
Author(s):  
Kavya Bhakuni ◽  
Niketa Yadav ◽  
Pannuru Venkatesu

This study unravels the effect of a novel solvent medium designed by amalgamation of macromolecular crowders and deep eutectic solvents (DESs) on bovine serum albumin (BSA).


2018 ◽  
Vol 74 ◽  
pp. 267-274 ◽  
Author(s):  
Monique Barreto Santos ◽  
Carlos Wanderlei Piler de Carvalho ◽  
Edwin Elard Garcia-Rojas

2011 ◽  
Vol 115 (42) ◽  
pp. 12306-12314 ◽  
Author(s):  
Yang Shu ◽  
Menglin Liu ◽  
Shuai Chen ◽  
Xuwei Chen ◽  
Jianhua Wang

2016 ◽  
Vol 5 (1) ◽  
pp. 331-339 ◽  
Author(s):  
Otávio Augusto Chaves ◽  
Edgar Schaeffer ◽  
Carlos Maurício R. Sant'Anna ◽  
José Carlos Netto-Ferreira ◽  
Dari Cesarin-Sobrinho ◽  
...  

Serum albumin is the most abundant protein in blood plasma; among its functions is the transport of a high variety of drugs in the body. Quinones show several biological and pharmacological activities, such as anti-malarial, antitumor, anti-microbial, anti-inflammatory and anti-parasitic. We report fluorescence and circular dichroism (CD) spectroscopic studies to try to understand the interaction process between α-lapachone (α-LAP) and bovine serum albumin (BSA). Studies using computational methods, such as molecular docking, were performed to identify the main cavity in which this interaction occurs as well as the type of intermolecular interactions between the amino acid residues from albumin and the ligand. The BSA fluorescence quenching by added α-LAP is a static process, indicating an initial association BSA: α-LAP. The Ka and Kb values for the interaction BSA: α-LAP are in the range 105-104 L∙mol-1, indicating a strong binding between these two species. CD data show that there is no significant perturbation on the secondary structure of the protein with binding. The negative ΔGo values are consistent with spontaneous binding occurring endothermically (ΔHo = 127 kJ∙mol-1), and possibly driven by hydrophobic factors (ΔSo = 0.526 kJ∙mol-1∙s-1). The number of binding sites (n) indicates the existence of just one main binding site in BSA for α-LAP, with molecular docking results showing that it binds preferentially to the albumin in the domain IIA, where the Trp-212 residue is located. The ligand interacts via hydrogen bond with Arg-259 and Tyr-149 residues and via T-stacking with the fluorophore Trp-212 residue.


2017 ◽  
Vol 41 (16) ◽  
pp. 8130-8139 ◽  
Author(s):  
Ayonbala Baral ◽  
Lakkoji Satish ◽  
Dipti P. Das ◽  
Harekrushna Sahoo ◽  
Malay K. Ghosh

Systematic experimental investigation of MnO2–BSA complexes in terms of the structure and stability of the protein as well as the aggregation of the nanoparticle.


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