PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33979725-1	2021	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	77-86	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-122	
33979725-3	2021	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	122-131	acetylcholinesterase (Cartwright blood group)	Homo sapiens	155-159	
33979725-3	2021	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	122-131	acetylcholinesterase (Cartwright blood group)	Homo sapiens	340-344	
33979725-3	2021	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	310-319	acetylcholinesterase (Cartwright blood group)	Homo sapiens	155-159	
34637680-0	2021	Probing the intermolecular interactions, binding affinity, charge density distribution and dynamics of silibinin in dual targets AChE and BACE1: QTAIM and molecular dynamics perspective.	Silybin	103-112	acetylcholinesterase (Cartwright blood group)	Homo sapiens	129-133	
34637680-3	2021	An experimental study reports that silibinin molecule inhibits both AChE and BACE1 enzymes.	Silybin	35-44	acetylcholinesterase (Cartwright blood group)	Homo sapiens	68-72	
34637680-4	2021	Present study aims to understand the dual binding mechanism of silibinin in the active site of AChE and BACE1 from the intermolecular interactions, conformational flexibility, charge density distribution, binding energy and the stability of molecule.	Silybin	63-72	acetylcholinesterase (Cartwright blood group)	Homo sapiens	95-99	
34637680-8	2021	The electrostatic potential map displays the electronegative/positive regions at the interaction zone of silibinin with AChE and BACE1 complexes.	Silybin	105-114	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-124	
34637680-9	2021	The MD simulation confirms that the silibinin molecule is stable in the active site of AChE and BACE1 enzymes.	Silybin	36-45	acetylcholinesterase (Cartwright blood group)	Homo sapiens	87-91