Modification of proteins with cyclodextrins prevents aggregation and surface adsorption and increases thermal stability.
Langmuir
; 27(21): 13091-6, 2011 Nov 01.
Article
em En
| MEDLINE
| ID: mdl-21902259
ABSTRACT
This work describes a general approach for preventing protein aggregation and surface adsorption by modifying proteins with ß-cyclodextrins (ßCD) 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).
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ribonuclease Pancreático
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Temperatura
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Muramidase
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Ciclodextrinas
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Multimerização Proteica
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article