Lone-pair–pi interactions: analysis of the physical origin and biolological implications
| Authors | |
|---|---|
| Year of publication | 2016 |
| Type | Article in Periodical |
| Magazine / Source | Physical Chemistry Chemical Physics |
| MU Faculty or unit | |
| Citation | |
| Web | DOI: 10.1039/C6CP01524G |
| Doi | http://dx.doi.org/10.1039/C6CP01524G |
| Field | Physical chemistry and theoretical chemistry |
| Keywords | lone-pair-pi interaction; anion-pi; DFT; energy decomposition analysis |
| Description | Lone-pair-pi (lp-pi) interactions have been suggested to stabilize DNA and protein structures, and to participate in the formation of DNA-protein complexes. To elucidate their physical origin, we have carried out a theoretical multi-approach analysis of two biologically relevant model systems, the water-indole and water-uracil complexes, which we compared with the structurally similar chloride-tetracyanobenzene (TCB) complex previously shown to contain a strong charge-transfer (CT) binding component. We demonstrate that the CT component in lp-pi interactions between water and indole/uracil is significantly smaller than that stabilizing the Cl-TCB reference system. The strong lp(Cl-)-pi(TCB)* orbital interaction is characterized by a small energy gap and an efficient lp-pi* overlap. In contrast, in lp-pi interactions between water and indole or uracil, the corresponding energy gap is larger and the overlap less efficient. As a result, water-uracil and water-indole interactions are weak forces composed by smaller contributions from electrostatics, polarization, dispersion, and charge transfer. In addition, indole exhibits a negative electrostatic potential at its pi-face, making lp-pi interactions less favorable than O-H···pi hydrogen bonding. Consequently, some of the water-tryptophan contacts observed in X-ray structures of proteins and previously interpreted as lp-pi interactions [Luisi et al., Proteins 2004, 57, 1-8], might in fact arise from O-H···pi hydrogen bonding. |
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