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The CH-π interaction in protein - carbohydrate binding: Bioinformatics and in vitro quantification.

08:00 EDT 24th March 2020 | BioPortfolio

Summary of "The CH-π interaction in protein - carbohydrate binding: Bioinformatics and in vitro quantification."

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-π 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-π interactions employing bioinformatics (data mining, structural analysis), several experimental (ITC, X-ray crystallography) and computational techniques. The Protein Data Bank (PDB) has been used as a source of structural data. 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-π stacking contribution to the overall binding energy ranges from 4 kcal/mol up to 8 kcal/mol. All the results show that the stacking CH-π interactions in protein-carbohydrate complexes can be considered to be a driving force of the binding in such  complexes.

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Name: Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
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