Strength and Character of R–X···π Interactions Involving Aromatic Amino Acid Sidechains in Protein-Ligand Complexes Derived from Crystal Structures in the Protein Data Bank
Year: 2017
Type: article
Abstract: Here, we investigate the strengths of R–X···π interactions, involving both chlorine and bromine, in model systems derived from protein-ligand complexes found in the PDB. We find that the strengths of these interactions can vary significantly, with binding energies ranging from −2.01 to −3.60 kcal/mol. Symmetry adapted perturbation theory (SAPT) analysis shows that, as would be expected, dispersion plays the largest role in stabilizing these R–X···π interactions, generally accounting for about 50% to 80% of attraction. R–Br···π interactions are, for the most part, found to be stronger than R–Cl···π interactions, although the relative geometries of the interacting pair and the halogen’s chemical environment can also have a strong impact. The two factors that have the strongest impact on the strength of these R–X···π interactions is the distance between the halogen and the phenyl plane as well as the size of the halogen σ-hole.
Source: Crystals
DOI: 10.3390/cryst7090273
Authors: Kevin Riley, Khanh-An Tran
Institution: Xavier University of Louisiana
Language: English
Subfield: Physical and Theoretical Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $2,534
Awards: BUILD at Xavier, Project Pathways II, G2070940364, Generation of Liver X Receptor Agonists with LXRb Subtype Selectivity using Modern Computational and Chemical Synthetic Methods, Research Initiation Award: Characterization of Crystal Structures of Novel Materials using State-of the-Art Computational Techniques and Applications, RISE Option II at Xavier University of Louisiana
OpenAlex ID: W2752436180