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 language | English (US) |
---|---|
Pages (from-to) | 13091-13096 |
Number of pages | 6 |
Journal | Langmuir |
Volume | 27 |
Issue number | 21 |
DOIs | |
State | Published - Nov 1 2011 |
ASJC Scopus subject areas
- General Materials Science
- Condensed Matter Physics
- Surfaces and Interfaces
- Spectroscopy
- Electrochemistry