Issue 5, 2011

Glutathione (GSH)-decorated magnetic nanoparticles for binding glutathione-S-transferase (GST) fusion protein and manipulating live cells

Abstract

Iron oxide-based magnetic nanoparticles (MNP) surface-decorated with glutathione (GSH) via a dopamine anchor bind to human α1-glutathione S-transferase (GST) with high affinity and specificity and are able to separate GST fusion proteins from cell lysates. Both the purified GST and the protein of interest (POI) preserve their innate properties. The conjugate of MNP and the GST fusion protein also enables magnetic manipulation of cells.

Graphical abstract: Glutathione (GSH)-decorated magnetic nanoparticles for binding glutathione-S-transferase (GST) fusion protein and manipulating live cells

Supplementary files

Article information

Article type
Edge Article
Submitted
20 Jan 2011
Accepted
17 Feb 2011
First published
03 Mar 2011

Chem. Sci., 2011,2, 945-948

Glutathione (GSH)-decorated magnetic nanoparticles for binding glutathione-S-transferase (GST) fusion protein and manipulating live cells

Y. Pan, M. J. C. Long, X. Li, J. Shi, L. Hedstrom and B. Xu, Chem. Sci., 2011, 2, 945 DOI: 10.1039/C1SC00030F

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements