scholarly journals Non-covalent loading of ionic liquid-functionalized nanoparticles for bovine serum albumin: experiments and theoretical analysis

RSC Advances ◽  
2019 ◽  
Vol 9 (33) ◽  
pp. 19114-19120 ◽  
Author(s):  
Xingang Jia ◽  
Xiaoling Hu ◽  
Wenzhen Wang ◽  
Chunbao Du
Keyword(s):  
Ionic Liquid ◽  
Bovine Serum Albumin ◽  
Theoretical Analysis ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Theoretical Calculations ◽  
Covalent Binding ◽  
Functionalized Nanoparticles

Non-covalent binding between nanosilica and bovine serum albumin has been illustrated by experiments and theoretical calculations.

Spectroscopic and docking studies on the interaction between pyrrolidinium based ionic liquid and bovine serum albumin

2014 ◽  
Vol 124 ◽  
pp. 349-356 ◽  
Author(s):  
Meena Kumari ◽  
Jitendra Kumar Maurya ◽  
Upendra Kumar Singh ◽  
Abbul Bashar Khan ◽  
Maroof Ali ◽  
...  
Keyword(s):  
Ionic Liquid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Docking Studies

Insights into the denaturation of bovine serum albumin with a thermo-responsive ionic liquid

Soft Matter ◽  
2014 ◽  
Vol 10 (33) ◽  
pp. 6161-6171 ◽  
Author(s):  
Wenlong Li ◽  
Peiyi Wu
Keyword(s):  
Phase Transition ◽  
Ionic Liquid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Heating And Cooling ◽  
Dynamic Phase ◽  
Dynamic Phase Transition

The dynamic phase transition and denaturation mechanism of [P4,4,4,4][SS]–BSA–D2O solution during heating and cooling processes.

The reaction of S-mercuric-N-dansylcysteine with acetylcholinesterase and butyrylcholinesterase

1989 ◽  
Vol 67 (7) ◽  
pp. 337-344 ◽  
Author(s):  
George Tomlinson ◽  
Evelyn M. Kinsch
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Bovine Serum ◽  
Covalent Binding ◽  
Serum Cholinesterase ◽  
Enzyme Molecule ◽  
Electrophorus Electricus ◽  
Sulphydryl Groups

S-mercuric-N-dansylcysteine was investigated as a potential probe of protein sulphydryl groups using bovine serum albumin, S-carboxymethyl – bovine serum albumin, lysozyme, and partially reduced lysozyme as test proteins. Criteria used to assess covalent binding through mercury-bridged mercaptide linkages include a finite reaction time (minutes to hours), abolition of the characteristic fluorescence spectrum following addition of a reducing agent, and failure to separate probe and protein after chromatography or electrophoresis. By these criteria, both Torpedo californica acetylcholinesterase and human serum cholinesterase (butyrylcholinesterase) contain four free sulphydryl groups per tetrameric enzyme molecule whereas Electrophorus electricus acetylcholinesterase has none. Labeled acetylcholinesterase and butyrylcholinesterase remain active and responsive to the inactivator Zn2+. Zn2+ promotes an increase in the fluorescence of bound S-mercuric-N-dansylcysteine, whereas activators such as Mg2+ or gallamine promote a decrease, suggesting that the label may be a useful probe of ligand-induced conformational changes. With T. californica acetylcholinesterase, but not with human serum cholinesterase, Zn2+ also promotes access to two additional groups that are reactive towards the sulphydryl reagent.Key words: acetylcholinesterase, serum cholinesterase, sulphydryl groups, S-mercuric-N-dansylcysteine.

NMR and DFT Insight into the Synergistic Role of Bovine Serum Albumin-Ionic Liquid for Multicomponent Cascade Aldol/Knoevenagel-thia-Michael/Michael Reactions in One Pot

ChemCatChem ◽  
2016 ◽  
Vol 8 (19) ◽  
pp. 3050-3056 ◽  
Author(s):  
Yogesh Thopate ◽  
Richa Singh ◽  
Arun K. Sinha ◽  
Vikash Kumar ◽  
Mohammad Imran Siddiqi
Keyword(s):  
Ionic Liquid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
One Pot ◽  
Michael Reactions ◽  
Insight Into
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