A Structured Monodisperse PEG for the Effective Suppression of Protein Aggregation

Autor:	Kazushi Kinbara, Mihoko Ui, Kota Adachi, Hidehito Tochio, Haruki Obara, Takahiro Muraoka, Nabanita Sadhukhan, Shunichi Kawasaki, Masahiro Shirakawa
Rok vydání:	2013
Předmět:	Models Molecular Protein Conformation Dispersity Supramolecular chemistry Proteins General Chemistry Polyethylene glycol General Medicine Protein aggregation Catalysis Polyethylene Glycols chemistry.chemical_compound Protein structure chemistry Chemical engineering PEG ratio Polymer chemistry Native state Lysozyme Protein Multimerization
Zdroj:	Angewandte Chemie. 125:2490-2494
ISSN:	0044-8249
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71f9d2111ac2833b21c056f16f183842 https://doi.org/10.1002/ange.201206563 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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