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Structure‐based discovery of a new affinity ligand to pancreatic α‐amylase
Author(s) -
Westerfors Maria,
Tedebark Ulf,
Andersson Hans O,
Öhrman Sara,
Choudhury Devapriya,
Ersoy Oguz,
Shinohara Yasuro,
Axén Andreas,
Carredano Enrique,
Baumann Herbert
Publication year - 2003
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.626
Subject(s) - elution , chemistry , surface plasmon resonance , virtual screening , ligand (biochemistry) , amylase , covalent bond , chromatography , alpha amylase , affinity chromatography , enzyme , combinatorial chemistry , biochemistry , drug discovery , organic chemistry , nanoparticle , materials science , nanotechnology , receptor
A ligand useful for affinity capture of porcine pancreatic α‐amylase was found by virtual screening of the commercially available compound data base MDL® Available Chemicals Directory. Hits from the virtual screening were investigated for binding by nuclear magnetic resonance (NMR) and surface plasmon resonance. Selected compounds were tested for inhibition of the enzyme using a NMR‐based assay. One of the binders found was covalently coupled to a chromatographic resin and a column, packed with this resin, could retain α‐amylase, which subsequently was eluted by introduction of the known inhibitor acarbose to the elution buffer. Copyright © 2003 John Wiley & Sons, Ltd.