Issue 10, 2013

Site-specific peptide and protein immobilization on surface plasmon resonance chips via strain-promoted cycloaddition

Abstract

Surface plasmon resonance (SPR) is a powerful label-free diagnostic tool to study biomolecular interactions. However, one of the drawbacks of SPR is the lack of controlled immobilization of ligands on the sensor surface. We have developed a modular platform for the fast, reagent-free and site-specific immobilization of azide-containing ligands by strain-promoted cycloaddition onto a cyclooctyne-modified SPR sensor surface. The usefulness of the concept was shown in a study with a papain model system, and up to 150 experiments were performed without loss of surface quality. Furthermore, azide-containing green fluorescent protein (GFP) was also effectively immobilized. Taken together, cyclooctyne-modified SPR chips enable smooth and site-selective immobilization of ligands and prove to be more robust than traditionally functionalized systems.

Graphical abstract: Site-specific peptide and protein immobilization on surface plasmon resonance chips via strain-promoted cycloaddition

Supplementary files

Article information

Article type
Paper
Submitted
06 Dec 2012
Accepted
12 Mar 2013
First published
12 Mar 2013
This article is Open Access
Creative Commons BY license

Lab Chip, 2013,13, 1863-1867

Site-specific peptide and protein immobilization on surface plasmon resonance chips via strain-promoted cycloaddition

A. E. M. Wammes, M. J. E. Fischer, N. J. de Mol, M. B. van Eldijk, F. P. J. T. Rutjes, J. C. M. van Hest and F. L. van Delft, Lab Chip, 2013, 13, 1863 DOI: 10.1039/C3LC41338A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements