Ontology highlight
ABSTRACT:
SUBMITTER: Cadez T
PROVIDER: S-EPMC7659976 | biostudies-literature | 2020 Oct
REPOSITORIES: biostudies-literature
Čadež Tena T Grgičević Ana A Ahmetović Ramiza R Barić Danijela D Hrvat Nikolina Maček NM Kovarik Zrinka Z Škorić Irena I
Molecules (Basel, Switzerland) 20201022 21
A library of amine, oxime, ether, epoxy and acyl derivatives of the benzobicyclo[3.2.1]octene were synthesized and evaluated as inhibitors of both human acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The majority of the tested compounds exhibited higher selectivity for BChE. Structural adjustment for AChE seems to have been achieved by acylation, and the furan ring opening of furo-benzobicyclo[3.2.1]octadiene results for compound <b>51</b> with the highest AChE affinity (IC<sub>50 ...[more]