Issue 40, 2015
From the journal:

Chemical Communications

Protein stabilization by an amphiphilic short monodisperse oligo(ethylene glycol)†

Nabanita Sadhukhan,a   Takahiro Muraoka,*ab   Mihoko Ui,a   Satoru Nagatoishi,c   Kouhei Tsumotocde  and  Kazushi Kinbara*a  

* Corresponding authors

a Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Japan
E-mail: kinbara@tagen.tohoku.ac.jp

b PRESTO, Japan Science and Technology Agency, 4-1-8, Honcho, Kawaguchi, Saitama 332-0012, Japan

c Department of Bioengineering, The University of Tokyo, Bunkyo-ku, Tokyo 108-8656, Japan

d Department of Chemistry and Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 108-8656, Japan

e Institute of Medical Science, The University of Tokyo, 4-6-1, Shirokanedai, Minato-ku, Tokyo 108-8639, Japan

Abstract

A short, monodisperse additive (octa(ethylene glycol) monophenyl ether) functions to suppress aggregation of thermally and chemically denatured lysozyme. Control studies with shorter and non-amphiphilic derivatives revealed that the amphiphilic structure is essential, and octa(ethylene glycol) is nearly the minimum chain length for amphiphilic poly(ethylene glycol)s to stabilize proteins.

Graphical abstract: Protein stabilization by an amphiphilic short monodisperse oligo(ethylene glycol)

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Article information

DOI
https://doi.org/10.1039/C4CC10301G
Article type
Communication
Submitted
24 Dec 2014
Accepted
06 Mar 2015
First published
12 Mar 2015

Chem. Commun., 2015,51, 8457-8460

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Protein stabilization by an amphiphilic short monodisperse oligo(ethylene glycol)

N. Sadhukhan, T. Muraoka, M. Ui, S. Nagatoishi, K. Tsumoto and K. Kinbara, Chem. Commun., 2015, 51, 8457 DOI: 10.1039/C4CC10301G

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