ArticleACS applied materials & interfaces2022
Polyvalent Glycan Quantum Dots as a Multifunctional Tool for Revealing Thermodynamic, Kinetic, and Structural Details of Multivalent Lectin-Glycan Interactions.
Article in ACS applied materials & interfaces, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- SpEchinoidin, a C-type lectin and a member of an expanded CTL family, is up-regulated by phagocytes in sea urchins responding to immune challenge.Developmental and comparative immunology · 2026Article
- Probing Glycan-Gold Nanoparticle Architectures: Glycan Type, Density, and Linker Length, Governing Multivalent Lectin Binding and Viral Inhibition.ACS applied materials & interfaces · 2026Article
- Article
- The brightness of lectins conjugated to quantum dots.Biophysical reviews · 2025Review
- Sugar-Coated: Can Multivalent Glycoconjugates Improve upon Nature's Design?Journal of the American Chemical Society · 2024Review
- Article
- Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Probing the pH-dependency of DC-SIGN/R multivalent lectin-glycan interactions using polyvalent glycan-gold nanoparticles.Nanoscale advances · 2024Article
- Polyvalent Nano-Lectin Potently Neutralizes SARS-CoV-2 by Targeting Glycans on the Viral Spike Protein.JACS Au · 2023Article
- Polyvalent Glycan Functionalized Quantum Nanorods as Mechanistic Probes for Shape-Selective Multivalent Lectin-Glycan Recognition.ACS applied nano materials · 2023Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multivalent lectin-glycan interactions (MLGIs) are widespread and vital for biology. Their binding biophysical and structural details are thus highly valuable, not only for the understanding of binding affinity and specificity mechanisms but also for guiding the design of multivalent therapeutics against specific MLGIs. However, effective techniques that can reveal all such details remain unavailable. We have recently developed polyvalent glycan quantum dots (glycan-QDs) as a new probe for MLGIs. Using a pair of closely related tetrameric viral-binding lectins, DC-SIGN and DC-SIGNR, as model examples, we have revealed and quantified their large affinity differences in glycan-QD binding are due to distinct binding modes: with simultaneous binding for DC-SIGN and cross-linking for DC-SIGNR. Herein, we further extend the capacity of the glycan-QD probes by investigating the correlation between binding mode and binding thermodynamics and kinetics and further probing a structural basis of their binding nature. We reveal that while both lectins' binding with glycan-QDs is enthalpy driven with similar binding enthalpy changes, DC-SIGN pays a lower binding entropy penalty, resulting in a higher affinity than DC-SIGNR. We then show that DC-SIGN binding gives a single second-order
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