A structured monodisperse PEG for the effective suppression of protein aggregation

Takahiro Muraoka, Kota Adachi, Mihoko Ui, Shunichi Kawasaki, Nabanita Sadhukhan, Haruki Obara, Hidehito Tochio, Masahiro Shirakawa, Kazushi Kinbara

Research output: Contribution to journalArticlepeer-review

51 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2430-2434
Number of pages5
JournalAngewandte Chemie - International Edition
Volume52
Issue number9
DOIs
Publication statusPublished - 2013 Feb 25

Keywords

  • enzymes
  • macrocycles
  • polyethylene glycol
  • protein manipulation
  • supramolecular chemistry

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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