Modification of proteins with cyclodextrins prevents aggregation and surface adsorption and increases thermal stability

Deepali Prashar, Dawei Cui, Debjyoti Bandyopadhyay, Yan Yeung Luk

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

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).

Original languageEnglish (US)
Pages (from-to)13091-13096
Number of pages6
JournalLangmuir
Volume27
Issue number21
DOIs
StatePublished - Nov 1 2011

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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