NMR evaluation of adipocyte fatty acid binding protein (aP2) with R- and S-ibuprofen.

摘要: Abstract We have examined global chemical shift perturbations for aP2 ligand complexes and compared these with amide temperature coefficients. Hydrogen bond potential was monitored by shift’s coefficient. Based on this information, we propose that the binding energy contribution can be spread out to multiple distant residues. For aP2, ability of receptor protein change its hydrogen interactions in β-strands accommodate different scaffolds seems make difficult structure based drug design. While stabilization differential bonds is likely small individual residues, accumulative effect may a dramatic impact affinity.