Journal
MOLECULES
Volume 22, Issue 7, Pages -Publisher
MDPI
DOI: 10.3390/molecules22071038
Keywords
carbohydrate-protein interactions; CH/pi interactions; lectins; interaction energy; non-canonical hydrogen bond
Funding
- Ministry of Education, Youth and Sports of the Czech Republic [LD13024, LD14133]
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Many carbohydrate-binding proteins contain aromatic amino acid residues in their binding sites. These residues interact with carbohydrates in a stacking geometry via CH/pi interactions. These interactions can be found in carbohydrate-binding proteins, including lectins, enzymes and carbohydrate transporters. Besides this, many non-protein aromatic molecules (natural as well as artificial) can bind saccharides using these interactions. Recent computational and experimental studies have shown that carbohydrate-aromatic CH/pi interactions are dispersion interactions, tuned by electrostatics and partially stabilized by a hydrophobic effect in solvated systems.
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