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Issue 15, 2011
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Modified peptide monolayer binding His-tagged biomolecules for small ligand screening with SPR biosensors

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Abstract

A peptide self-assembled monolayer (SAM) was designed to bind His-tagged biomolecules for surface plasmon resonance (SPR) bioanalysis, which was applied for the determination of Kd for small ligand screening against CD36. Nonspecific adsorption could be minimized using penta- and hexa-peptide monolayers. In particular, monolayers consisting of 3-mercaptopropionyl-leucinyl-histidinyl-aspartyl-leucinyl-histidinyl-aspartic acid (3-Mpa-LHDLHD) exhibited little (12 ng cm−2) nonspecific adsorption in crude serum. Modification of this peptide monolayer with Nα,Nα-bis(carboxymethyl)-L-lysine gave a surface competent for binding His-tagged proteins, as demonstrated using enzyme (human dihydrofolate reductase), protein/antibody and receptor (CD36) examples. Immobilization featured chelation of copper and the His-tagged protein by the peptide monolayer, which could be recycled by removing the copper using imidazole washes prior to reuse.

Graphical abstract: Modified peptide monolayer binding His-tagged biomolecules for small ligand screening with SPR biosensors

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Supplementary files

Article information


Submitted
23 Mar 2011
Accepted
05 May 2011
First published
23 Jun 2011

Analyst, 2011,136, 3142-3148
Article type
Paper

Modified peptide monolayer binding His-tagged biomolecules for small ligand screening with SPR biosensors

O. R. Bolduc, P. Lambert-Lanteigne, D. Y. Colin, S. S. Zhao, C. Proulx, D. Boeglin, W. D. Lubell, J. N. Pelletier, J. Féthière, H. Ong and J. Masson, Analyst, 2011, 136, 3142
DOI: 10.1039/C1AN15235A

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