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Back‐Scattering Interferometry: An Ultrasensitive Method for the Unperturbed Detection of Acetylcholinesterase–Inhibitor Interactions
Author(s) -
Haddad Gabrielle L.,
Young Sherri C.,
Heindel Ned D.,
Bornhop Darryl J.,
Flowers Robert A.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201203640
Subject(s) - acetylcholinesterase , interferometry , scattering , enzyme , substrate (aquarium) , aché , computer science , chemistry , enzyme inhibition , computational biology , biochemistry , nanotechnology , combinatorial chemistry , physics , materials science , optics , biology , ecology
A series of inhibitors of acetylcholinesterase (AChE) have been screened by back‐scattering interferometry (BSI). Enzyme levels as low as 100 p M (22 000 molecules of AChE) can be detected. This method can be used to screen for mixed AChE inhibitors, agents that have shown high efficacy against Alzheimer's disease, by detecting dual‐binding interactions. E=enzyme, I=inhibitor, S=substrate.