Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 55, Issue 15, Pages 4738-4742Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201600593
Keywords
carbohydrates; FRET; proteins; quantum dots; viral inhibition
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Funding
- Wellcome Trust (UK) [097354/Z/11/Z]
- Khon Kaen University scholarship (Thailand)
- BBSRC [BB/M005666/1]
- Biotechnology and Biological Sciences Research Council [BB/M005666/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/K039202/1] Funding Source: researchfish
- BBSRC [BB/M005666/1] Funding Source: UKRI
- EPSRC [EP/K039202/1] Funding Source: UKRI
- Wellcome Trust [097354/Z/11/Z] Funding Source: Wellcome Trust
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A highly efficient cap-exchange approach for preparing compact, dense polyvalent mannose-capped quantum dots (QDs) has been developed. The resulting QDs have been successfully used to probe multivalent interactions of HIV/Ebola receptors DC-SIGN and DC-SIGNR (collectively termed as DC-SIGN/R) using a sensitive, ratiometric Forster resonance energy transfer (FRET) assay. The QD probes specifically bind DC-SIGN, but not its closely related receptor DC-SIGNR, which is further confirmed by its specific blocking of DC-SIGN engagement with the Ebola virus glycoprotein. Tuning the QD surface mannose valency reveals that DC-SIGN binds more efficiently to densely packed mannosides. A FRET-based thermodynamic study reveals that the binding is enthalpy-driven. This work establishes QD FRET as a rapid, sensitive technique for probing structure and thermodynamics of multivalent protein-ligand interactions.
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