Title : Identification of potential bivalent inhibitors from natural compounds for acetylcholinesterase through in silico screening using multiple pharmacophores.

Pub. Date : 2013 Mar

PMID : 23353586






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 The AD pathogenicity involved in AChE protein is mainly due to amyloid beta peptide aggregation, which is triggered specifically by peripheral anionic site (PAS) of AChE. Aminosalicylic Acid acetylcholinesterase (Cartwright blood group) Homo sapiens
2 The AD pathogenicity involved in AChE protein is mainly due to amyloid beta peptide aggregation, which is triggered specifically by peripheral anionic site (PAS) of AChE. Aminosalicylic Acid acetylcholinesterase (Cartwright blood group) Homo sapiens
3 In the present study, a workflow has been developed for the identification and prioritization of potential compounds that could interact not only with the catalytic site but also with the PAS of AChE. Aminosalicylic Acid acetylcholinesterase (Cartwright blood group) Homo sapiens
4 The knowledge gained from this study, could lead to the discovery of potential AChE inhibitors that are highly specific for AD treatment as they are bivalent lead molecules endowed with dual binding ability for both catalytic site and PAS of AChE. Aminosalicylic Acid acetylcholinesterase (Cartwright blood group) Homo sapiens
5 The knowledge gained from this study, could lead to the discovery of potential AChE inhibitors that are highly specific for AD treatment as they are bivalent lead molecules endowed with dual binding ability for both catalytic site and PAS of AChE. Aminosalicylic Acid acetylcholinesterase (Cartwright blood group) Homo sapiens