title: Modification of proteins with cyclodextrins prevents aggregation and surface adsorption and increases thermal stability.
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).
authors: Department of Chemistry, Syracuse University, Syracuse, New York 13244, United States.
authors: Deepali
authors: D
authors: Prashar
authors: DaWei
authors: D
authors: Cui
authors: Debjyoti
authors: D
authors: Bandyopadhyay
authors: Yan-Yeung
authors: YY
authors: Luk
mesh_terms: D000327:Adsorption; D000818:Animals; D003505:Cyclodextrins / Q000378:metabolism*; D008239:Lysine; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D055503:Protein Multimerization; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000378:metabolism*; D013499:Surface Properties; D013696:Temperature; D014867:Water / Q000737:chemistry
chemical_list: D003505:Cyclodextrins; D014867:Water; D012259:Ribonuclease, Pancreatic; D009113:Muramidase; D008239:Lysine