ArticleJournal of the American Chemical Society2024
Dissecting the Conformational Stability of a Glycan Hairpin.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Cis glycan-glycan interactions organize membrane nanodomains that tune receptor signaling.Nature communications · 2026Article
- Carbohydrate Physicochemical Properties: The Innate Hydrogen Bond Donating Capacities of α-Glucoside and α-Galactoside Alcohol Groups.Angewandte Chemie (International ed. in English) · 2026Article
- Leveraging Glycan-Glycan Interactions to Tune the Conformation of Glycan Hairpins and Build Rigid 3D Architectures.Journal of the American Chemical Society · 2026Article
- Article
- Rapid and Reliable Conformational Analysis of Glycans by Small Angle X-Ray Scattering Guided Molecular Dynamics Simulations.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Total Synthesis and Anomeric Configuration Revision of Zwitterionic Polysaccharide A2's Pentasaccharide Repeating Unit fromJACS Au · 2025Article
- Glycosaminoglycans as Polyelectrolytes: Charge, Interactions, and Applications.Chembiochem : a European journal of chemical biology · 2025Review
- Stapling of β-Glucans Increases Antibody Binding.Journal of the American Chemical Society · 2025Article
- Acceptor-Adaptive Automated Glycosylation Optimization for Automated Glycan Assembly.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- A glycan foldamer that uses carbohydrate-aromatic interactions to perform catalysis.Nature chemistry · 2025Article
- Controlling Glycan Folding with Ionic Functional Groups.Journal of the American Chemical Society · 2025Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Systematic structural studies of model oligopeptides revealed important aspects of protein folding and offered design principles to access non-natural materials. In the same way, the rules that regulate glycan folding could be established by studying synthetic oligosaccharide models. However, their analysis is often limited due to the synthetic and analytical complexity. By utilizing a glycan capable of spontaneously folding into a hairpin conformation as a model system, we investigated the factors that contribute to its conformational stability in aqueous solution. The modular design of the hairpin model featured a trisaccharide turn unit and two β-1,4-oligoglucoside stacking strands that allowed for systematic chemical modifications of the glycan sequence, including the introduction of NMR labels and staples. Nuclear magnetic resonance assisted by molecular dynamics simulations revealed that stereoelectronic effects and multiple glycan-glycan interactions are the major determinants of folding stabilization. Chemical modifications in the glycan primary sequence (e.g., strand elongation) can be employed to fine-tune the rigidity of structural motifs distant from the modification sites. These results could inspire the design of other glycan architectures, with implications in glycobiology and material sciences.
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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.