ArticleJournal of the American Chemical Society2016
The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 52 citations in OpenAlex.
- The energetic landscape of CH-π interactions in protein-carbohydrate binding.Chemical science · 2025Article
- Tools for structural lectinomics: From structures to lectomes.BBA advances · 2025Article
- Article
- Soluble Human Lectins at the Host-Microbe Interface.Annual review of biochemistry · 2024Review
- A Computational and Chemical Design Strategy for Manipulating Glycan-Protein Recognition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Extending the Martini 3 Coarse-Grained Force Field to Carbohydrates.Journal of chemical theory and computation · 2022Article
- Exploiting non-covalent interactions in selective carbohydrate synthesis.Nature reviews. Chemistry · 2021Review
- CH-π Interactions in Glycan Recognition.ACS chemical biology · 2021Review
- Development and Evaluation of GlycanDock: A Protein-Glycoligand Docking Refinement Algorithm in Rosetta.The journal of physical chemistry. B · 2021Article
- Stereoelectronic effects in stabilizing protein-N-glycan interactions revealed by experiment and machine learning.Nature chemistry · 2021Article
- Synthetic Carbohydrate Chemistry and Translational Medicine.The Journal of organic chemistry · 2020Article
- Three-Dimensional Structures of Carbohydrates and Where to Find Them.International journal of molecular sciences · 2020Review
- Structure and Dynamics of N-Glycosylated Human Ribonuclease 1.Biochemistry · 2020Article
- Modulation of the NOD-like receptors NOD1 and NOD2: A chemist's perspective.Bioorganic & medicinal chemistry letters · 2019Review
- Oligosaccharide Synthesis and Translational Innovation.Journal of the American Chemical Society · 2019Review
- Predicting the Structures of Glycans, Glycoproteins, and Their Complexes.Chemical reviews · 2018Review
- Structure-based discovery of glycomimetic FmlH ligands as inhibitors of bacterial adhesion during urinary tract infection.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Chemically Precise Glycoengineering Improves Human Insulin.ACS chemical biology · 2018Article
- Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase fromBiotechnology for biofuels · 2018Article
- Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.Accounts of chemical research · 2017Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Interactions between proteins and carbohydrates are ubiquitous in biology. Therefore, understanding the factors that determine their affinity and selectivity are correspondingly important. Herein, we have determined the relative strengths of intramolecular interactions between a series of monosaccharides and an aromatic ring close to the glycosylation site in an N-glycoprotein host. We employed the enhanced aromatic sequon, a structural motif found in the reverse turns of some N-glycoproteins, to facilitate face-to-face monosaccharide-aromatic interactions. A protein host was used because the dependence of the folding energetics on the identity of the monosaccharide can be accurately measured to assess the strength of the carbohydrate-aromatic interaction. Our data demonstrate that the carbohydrate-aromatic interaction strengths are moderately affected by changes in the stereochemistry and identity of the substituents on the pyranose rings of the sugars. Galactose seems to make the weakest and allose the strongest sugar-aromatic interactions, with glucose, N-acetylglucosamine (GlcNAc) and mannose in between. The NMR solution structures of several of the monosaccharide-containing N-glycoproteins were solved to further understand the origins of the similarities and differences between the monosaccharide-aromatic interaction energies. Peracetylation of the monosaccharides substantially increases the strength of the sugar-aromatic interaction in the context of our N-glycoprotein host. Finally, we discuss our results in light of recent literature regarding the contribution of electrostatics to CH-π interactions and speculate on what our observations imply about the absolute conservation of GlcNAc as the monosaccharide through which N-linked glycans are attached to glycoproteins in eukaryotes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.