Issue 26, 2013
From the journal:

Chemical Communications

A generalized strategy for immobilizing uniformly oriented membrane proteins at solid interfaces†

Amit Vaish,*ab   Vitalii Silin,ab   Marlon L. Walker,c   Kristen L. Steffens,c   Susan Krueger,a   Alexei A. Yeliseev,d   Klaus Gawrischd  and  David J. Vanderah*e  

* Corresponding authors

a National Institute of Standards and Technology (NIST) Center for Neutron Research, Gaithersburg, USA
E-mail: amit.vaish@nist.gov

b Department of Materials Science and Engineering, University of Maryland, College Park, USA

c Materials Measurement Laboratory, NIST, Gaithersburg, USA

d Laboratory of Membrane Biochemistry and Biophysics, National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Bethesda, Maryland, USA

e Institute for Bioscience and Biotechnology Research, NIST, Rockville, USA
E-mail: vanderah@ibbr.umd.edu

Abstract

We have developed a method based on self-assembly of thiols on Au substrates to immobilize membrane proteins at interfaces. Using water soluble nitrilotriacetic acid (NTA)-terminated oligo(ethylene glycol) thiols, a histidine-tagged G protein-coupled membrane receptor (GPCR) was captured in a defined orientation with little nonspecific binding.

Graphical abstract: A generalized strategy for immobilizing uniformly oriented membrane proteins at solid interfaces

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Article information

DOI
https://doi.org/10.1039/C3CC00077J
Article type
Communication
Submitted
04 Jan 2013
Accepted
13 Feb 2013
First published
25 Feb 2013

Chem. Commun., 2013,49, 2685-2687

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A generalized strategy for immobilizing uniformly oriented membrane proteins at solid interfaces

A. Vaish, V. Silin, M. L. Walker, K. L. Steffens, S. Krueger, A. A. Yeliseev, K. Gawrisch and D. J. Vanderah, Chem. Commun., 2013, 49, 2685 DOI: 10.1039/C3CC00077J

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