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.
Vancomycin dimer formation between analogues of bacterial peptidoglycan surfaces probed by force spectroscopy
Batchelor, Matthew,Zhou, Dejian,Cooper, Matthew A.,Abell, Chris,Rayment, Trevor
supporting information; experimental part, p. 1142 - 1148 (2010/06/15)
Functionalised thiols presenting peptides found in the peptidoglycan of vancomycin-sensitive and -resistant bacteria were synthesised and used to form self-assembled monolayers (SAMs) on gold surfaces. This model bacterial cell-wall surface mimic was used to study binding interactions with vancomycin. Force spectroscopy, using the atomic force microscope (AFM), was used to investigate the specific rupture of interfacial vancomycin dimer complexes formed between pairs of vancomycin molecules bound to peptide-coated AFM probe and substrate surfaces. Clear adhesive contacts were observed between the vancomycin-sensitive peptide surfaces when vancomycin was present in solution, and the adhesion force demonstrated a clear dependence on antibiotic concentration. The Royal Society of Chemistry.
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.
