Title : Binding studies of known molecules with acetylcholinesterase and bovine serum albumin: A comparative view.

Pub. Date : 2021 Oct 5

PMID : 33979725






4 Functional Relationships(s)
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1 The interactions between selected molecules (piperine, tacrine, curcumin and silibinin) and proteins (acetylcholinesterase and bovine serum albumin) were investigated by Fluorescence spectroscopy, molecular docking, molecular dynamics, free energy calculation and non-covalent interaction analysis. Silybin acetylcholinesterase (Cartwright blood group) Homo sapiens
2 The steady-state emission spectrum results showed that presence of static quenching mode for piperine, tacrine, curcumin, silibinin molecules with BSA and AChE complexes separately and this excitation-emission matrix analysis suggest that formation of ground-state complex between piperine, tacrine, curcumin, silibinin drugs and both BSA, AChE protein molecules. Silybin acetylcholinesterase (Cartwright blood group) Homo sapiens
3 The steady-state emission spectrum results showed that presence of static quenching mode for piperine, tacrine, curcumin, silibinin molecules with BSA and AChE complexes separately and this excitation-emission matrix analysis suggest that formation of ground-state complex between piperine, tacrine, curcumin, silibinin drugs and both BSA, AChE protein molecules. Silybin acetylcholinesterase (Cartwright blood group) Homo sapiens
4 The steady-state emission spectrum results showed that presence of static quenching mode for piperine, tacrine, curcumin, silibinin molecules with BSA and AChE complexes separately and this excitation-emission matrix analysis suggest that formation of ground-state complex between piperine, tacrine, curcumin, silibinin drugs and both BSA, AChE protein molecules. Silybin acetylcholinesterase (Cartwright blood group) Homo sapiens