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Updated: May 29, 2026

4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Modification of proteins with cyclodextrins prevents aggregation and surface adsorption and increases thermal
Deepali Prashar1, DaWei Cui, Debjyoti Bandyopadhyay
1Department of Chemistry, Syracuse University, Syracuse, New York 13244, United States.
Abstract:
This work describes a general approach for preventing protein aggregation and surface adsorption by modifying proteins with β-cyclodextrins (βCD) via an efficient water-driven ligation. As compared to native unmodified proteins, the cyclodextrin-modified proteins (lysozyme and RNase A) exhibit significant reduction in aggregation, surface adsorption and increase in thermal stability. These results reveal a new chemistry for preventing protein aggregation and surface adsorption that is likely of different mechanisms than that by modifying proteins with poly(ethylene glycol).
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