We applied this method to examine the binding affinity for a series of published cyclin-dependent kinase 2 (CDK2) inhibitors.
Notable features of the present structural model include: (1) parameterization of the Mg2+ hexacoordination system using ab initio quantum chemical calculations to accurately represent the ATP-kinase interaction; and (2) comparison between the docking scores and measured binding affinities for a series of oxindole-based Pfmrk inhibitors of known activity.
The preliminary pharmacological evaluation revealed a nanomolar AT1 receptor binding affinity for all compounds in the series, and a potent antagonistic activity in an isolated rabbit aortic strip functional assay for compounds 6f, 6g, 6h and 6k was also demonstrated.
The aim of this study is to propose a series of novel [60] fullerene-based inhibitors with optimal binding affinity for the HIV-1 PR enzyme.
In 2010, Bing et al. described the streptavidin-binding aptamer St-2-1 and a series of St-2-1-derived mutated sequences and their binding affinity for streptavidin measured in a competition assay with FAM-labeled St-2-1.
To define the roles of individual bases of the direct-repeat motifs in binding PhoP, we designed a series of DNA sequences with mutations in the motifs and analyzed their binding affinity for PhoP by ITC (Table 1).
We found that, in the peptide series, the extent of c-Src activation is directly correlated to the respective binding affinity for Src-SH2.
A series of novel arylpiperazines bearing a 3,3-diphenylpyrrolidin-2-one 3,3-diphenylpyrrolidin-2-one 3,3-diphenylpyrrolidin-2-one 3,3-diphenylpyrrolidin-2-onenoceptors (ARs), as well as their antiarrhythmic, and antihypertensive activities.
To confirm the role of the repeat motifs in binding specificity, we designed a series of duplex DNA sequences based on the dominant sequence identified from SELEX experiments and assayed their binding affinity for PhoP by an EMSA.
