J 2016

Lone-pair–pi interactions: analysis of the physical origin and biolological implications

NOVOTNÝ, Jan, Sophia BAZZI, Radek MAREK and Jiří KOZELKA

Basic information

Original name

Lone-pair–pi interactions: analysis of the physical origin and biolological implications

Authors

NOVOTNÝ, Jan (203 Czech Republic, belonging to the institution), Sophia BAZZI (364 Islamic Republic of Iran, belonging to the institution), Radek MAREK (203 Czech Republic, belonging to the institution) and Jiří KOZELKA (250 France, guarantor, belonging to the institution)

Edition

Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2016, 1463-9076

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10403 Physical chemistry

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 4.123

RIV identification code

RIV/00216224:14310/16:00087988

Organization unit

Faculty of Science

DOI

UT WoS

000379939100089

Keywords in English

lone-pair-pi interaction; anion-pi; DFT; energy decomposition analysis

Tags

Tags

International impact, Reviewed
Změněno: 18/9/2019 14:45, prof. RNDr. Radek Marek, Ph.D.

Abstract

V originále

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.

Links

GA14-14654S, research and development project
Name: Studium fyzikální podstaty interakcí lone-pair-pi v biomolekulárních systémech. Role interakcí lone-pair-pi při stabilizaci proteinu Engrailed (Acronym: Lone-pair-pi interactions)
Investor: Czech Science Foundation
LQ1601, research and development project
Name: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR