The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00114712" target="_blank" >RIV/00216224:14740/20:00114712 - isvavai.cz</a>

Result on the web

<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.202000593" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.202000593</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/chem.202000593" target="_blank" >10.1002/chem.202000593</a>

Result language

angličtina

Original language name

The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification

Original language description

The molecular recognition of carbohydrates by proteins plays a key role in many biological processes including immune response, pathogen entry into a cell, and cell-cell adhesion (e.g., in cancer metastasis). Carbohydrates interact with proteins mainly through hydrogen bonding, metal-ion-mediated interaction, and non-polar dispersion interactions. The role of dispersion-driven CH-pi interactions (stacking) in protein-carbohydrate recognition has been underestimated for a long time considering the polar interactions to be the main forces for saccharide interactions. However, over the last few years it turns out that non-polar interactions are equally important. In this study, we analyzed the CH-pi interactions employing bioinformatics (data mining, structural analysis), several experimental (isothermal titration calorimetry (ITC), X-ray crystallography), and computational techniques. The Protein Data Bank (PDB) has been used as a source of structural data. The PDB contains over 12 000 protein complexes with carbohydrates. Stacking interactions are very frequently present in such complexes (about 39 % of identified structures). The calculations and the ITC measurement results suggest that the CH-pi stacking contribution to the overall binding energy ranges from 4 up to 8 kcal mol(-1). All the results show that the stacking CH-pi interactions in protein-carbohydrate complexes can be considered to be a driving force of the binding in such complexes.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10600 - Biological sciences

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Chemistry - A European Journal

ISSN

0947-6539

e-ISSN

—

Volume of the periodical

26

Issue of the periodical within the volume

47

Country of publishing house

CH - SWITZERLAND

Number of pages

12

Pages from-to

10769-10780

UT code for WoS article

000552350100001

EID of the result in the Scopus database

2-s2.0-85088650259