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A structured monodisperse PEG for the effective suppression of protein aggregation.
Muraoka, Takahiro; Adachi, Kota; Ui, Mihoko; Kawasaki, Shunichi; Sadhukhan, Nabanita; Obara, Haruki; Tochio, Hidehito; Shirakawa, Masahiro; Kinbara, Kazushi.
Afiliação
  • Muraoka T; Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Sendai, Japan.
Angew Chem Int Ed Engl ; 52(9): 2430-4, 2013 Feb 25.
Article em En | MEDLINE | ID: mdl-23361965
Part of the solution: A PEG with a discrete triangular structure exhibits hydrophilicity/hydrophobicity switching upon increasing temperatures, and suppresses the thermal aggregation of lysozyme to retain nearly 80 % of the enzymatic activity. CD and NMR spectroscopic studies revealed that, with the structured PEG, the higher-order structures of lysozyme persist at high temperature, and the native conformation is recovered after cooling.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polietilenoglicóis / Proteínas Idioma: En Revista: Angew Chem Int Ed Engl Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Japão

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polietilenoglicóis / Proteínas Idioma: En Revista: Angew Chem Int Ed Engl Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Japão