Issue 40, 2014
From the journal:

Chemical Communications

Enhanced activity and stability of organophosphorus hydrolase via interaction with an amphiphilic polymer†

Minkyu Kim,a   Manos Gkikas,a   Aaron Huang,a   Jeon Woong Kang,b   Nisaraporn Suthiwangcharoen,c   Ramanathan Nagarajanc  and  Bradley D. Olsen*a  

* Corresponding authors

a Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
E-mail: bdolsen@mit.edu

b Laser Biomedical Research Center, G. R. Harrison Spectroscopy Laboratory, Massachusetts Institute of Technology, Cambridge, MA, USA

c Molecular Sciences and Engineering Team, Natick Soldier Research, Development & Engineering Center, Natick, MA 01760, USA

Abstract

A simple approach to enhancing the activity and stability of organophosphorus hydrolase (OPH) is developed based on interactions between the hydrophobic poly(propylene oxide) (PPO) block of amphiphilic Pluronics and the enzyme. This strategy provides an efficient route to new formulations for decontaminating organophosphate neurotoxins.

Graphical abstract: Enhanced activity and stability of organophosphorus hydrolase via interaction with an amphiphilic polymer

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Article information

DOI
https://doi.org/10.1039/C3CC47675H
Article type
Communication
Submitted
07 lis 2013
Accepted
07 vlj 2014
First published
21 vlj 2014

Chem. Commun., 2014,50, 5345-5348

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Enhanced activity and stability of organophosphorus hydrolase via interaction with an amphiphilic polymer

M. Kim, M. Gkikas, A. Huang, J. W. Kang, N. Suthiwangcharoen, R. Nagarajan and B. D. Olsen, Chem. Commun., 2014, 50, 5345 DOI: 10.1039/C3CC47675H

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