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Crystals 2017, 7(9), 273; doi:10.3390/cryst7090273

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

Department of Chemistry, Xavier University of Louisiana, New Orleans, LA 70125, USA
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Author to whom correspondence should be addressed.
Academic Editors: Peter Politzer and Jane S. Murray
Received: 1 July 2017 / Revised: 18 August 2017 / Accepted: 30 August 2017 / Published: 8 September 2017
(This article belongs to the Special Issue Analysis of Halogen and Other σ-Hole Bonds in Crystals)
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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. View Full-Text
Keywords: R–X···π; halogen bond; protein-ligand; drug design; halogen···π; noncovalent interaction R–X···π; halogen bond; protein-ligand; drug design; halogen···π; noncovalent interaction
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Riley, K.E.; Tran, K.-A. 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. Crystals 2017, 7, 273.

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