130727-45-6Relevant articles and documents
A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance
Sigal, George B.,Bamdad, Cynthia,Barberis, Alcide,Strominger, Jack,Whitesides, George M.
, p. 490 - 497 (1996)
This paper reports the generation of a self-assembled monolayer (SAM) that selectively binds proteins whose primary sequence terminates with a His-tag: a stretch of six histidines commonly incorporated in recombinant proteins to simplify purification. The SAM was prepared by the adsorption onto a gold surface of a mixture of two alkanethiols: one thiol that terminated with a nitrilotriacetic acid (NTA) group, a group that forms a tetravalent chelate with Ni(II), and a second thiol that terminated with a tri(ethylene glycol) group, a group that resists protein adsorption. His-tagged proteins bound to the SAM by interaction of the histidines with the two vacant sites on Ni(II) ions chelated to the surface NTA groups. Studies with model proteins showed the binding was specific for His-tagged proteins and required the presence of Ni(II) on the surface. Immobilized His-tagged proteins were kinetically stable in buffered saline at pH 7.2 but could be desorbed by treatment with 200 mM imidazole. Surface plasmon resonance studies for two model systems showed that His-tagged proteins adsorbed on the NTASAM retained a greater ability to participate hi binding interactions with proteins in solution than proteins immobilized in a thin dextran gel layer by covalent coupling.
Synthesis of benzaldehyde-functionalized glycans: A novel approach towards glyco-SAMs as a tool for surface plasmon resonance studies
Kopitzki, Sebastian,Jensen, Knud J.,Thiem, Joachim
experimental part, p. 7017 - 7029 (2010/09/10)
In recent years the interest in tools for investigating carbohydrateprotein (CPI) and carbohydrate-carbohydrate interactions (CCI) has increased significantly. For the investigation of CPI and CCI, several techniques employing different linking methods are available. Surface plasmon resonance (SPR) imaging is a most appropriate tool for analyzing the formation of self-assembled monolayers (SAM) of carbohydrate derivatives, which can mimic the glycocalyx. In contrast to the SPR imaging methods used previously to analyze CPI and CCI, the novel approach reported herein allows a facile and rapid synthesis of linker spacers and carbohydrate derivatives and enhances the binding event by controlling the amount and orientation of ligand. For immobilization on biorepulsive amino-functionalized SPR chips by reductive amination, diverse aldehyde-functionalized glycan structures (glucose, galactose, mannose, glucosamine, cellobiose, lactose, and lactosamine) have been synthesized in several facile steps that include olefin metathesis. Effective immobilization and the first binding studies are presented for the lectin concanavalin A.
Synthesis of a photo-caged aminooxy alkane thiol
Mancini, Rock J.,Li, Ronald C.,Tolstyka, Zachary P.,Maynard, Heather D.
experimental part, p. 4954 - 4959 (2010/02/16)
A photo-caged aminooxy alkane thiol synthesized in 7 steps and 15% overall yield was used to form a self-assembled monolayer (SAM). Photo-deprotection on the surface was confirmed by FT-IR spectroscopy and contact angle goniometry. Conjugation of a small molecule ketone, ethyl levulinate, further confirmed the presence of aminooxy groups on the surface. The Royal Society of Chemistry 2009.