ArticleBioorganic & medicinal chemistry letters2014
Protein-ligand interactions: probing the energetics of a putative cation-π interaction.
Article in Bioorganic & medicinal chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain.Bioorganic & medicinal chemistry letters · 2021Article
- Some thermodynamic effects of varying nonpolar surfaces in protein-ligand interactions.European journal of medicinal chemistry · 2020Article
- Thermodynamic consequences of Tyr to Trp mutations in the cation-π-mediated binding of trimethyllysine by the HP1 chromodomain.Chemical science · 2020Article
- Structural and functional properties of Grb2 SH2 dimer in CD28 binding.Biophysics and physicobiology · 2019Article
- Natural Products and Their Mimics as Targets of Opportunity for Discovery.The Journal of organic chemistry · 2017Article
- Probing the role of cation-π interaction in the thermotolerance and catalytic performance of endo-polygalacturonases.Scientific reports · 2016Article
- Conformational Ensemble of hIAPP Dimer: Insight into the Molecular Mechanism by which a Green Tea Extract inhibits hIAPP Aggregation.Scientific reports · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
In order to probe the energetics associated with a putative cation-π interaction, thermodynamic parameters are determined for complex formation between the Grb2 SH2 domain and tripeptide derivatives of RCO-pTyr-Ac6c-Asn wherein the R group is varied to include different alkyl, cycloalkyl, and aryl groups. Although an indole ring is reputed to have the strongest interaction with a guanidinium ion, binding free energies, ΔG°, for derivatives of RCO-pTyr-Ac6c-Asn bearing cyclohexyl and phenyl groups were slightly more favorable than their indolyl analog. Crystallographic analysis of two complexes reveals that test ligands bind in similar poses with the notable exception of the relative orientation and proximity of the phenyl and indolyl rings relative to an arginine residue of the domain. These spatial orientations are consistent with those observed in other cation-π interactions, but there is no net energetic benefit to such an interaction in this biological system. Accordingly, although cation-π interactions are well documented as important noncovalent forces in molecular recognition, the energetics of such interactions may be mitigated by other nonbonded interactions and solvation effects in protein-ligand associations.
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