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

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TitleA generalized strategy for immobilizing uniformly oriented membrane proteins at solid interfaces.
Publication TypeJournal Article
Year of Publication2013
AuthorsVaish, A, Silin, VI, Walker, ML, Steffens, KL, Krueger, S, Yeliseev, AA, Gawrisch, K, Vanderah, DJ
JournalChem Commun (Camb)
Volume49
Issue26
Pagination2685-7
Date Published2013 Apr 4
ISSN1364-548X
KeywordsEthylene Glycol, Gold, Models, Molecular, Molecular Structure, Nitrilotriacetic Acid, Receptors, G-Protein-Coupled, Solubility, Sulfhydryl Compounds, Surface Properties, Water
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.

DOI10.1039/c3cc00077j
Alternate JournalChem. Commun. (Camb.)
PubMed ID23435270
Grant List / / Intramural NIH HHS / United States