Structure-based discovery of a new affinity ligand to pancreatic α-amylase.

Autor: Maria Westerfors, Ulf Tedebark, Hans O Andersson, Sara Öhrman, Devapriya Choudhury, Oguz Ersoy, Yasuro Shinohara, Andreas Axén, Enrique Carredano, Herbert Baumann
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Zdroj: Journal of Molecular Recognition; Nov/Dec2003, Vol. 16 Issue 6, p396-405, 10p
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index