Affinity-based Protein Surface Pattern Formation by Ligand Self-Selection from Mixed Protein Solutions.

ABSTRACT: Photolithographically prepared surface patterns of two affinity ligands (biotin and chloroalkane) specific for two proteins (streptavidin and HaloTag®, respectively) are used to spontaneously form high-fidelity surface patterns of the two proteins from their mixed solution. High affinity protein-surface self-selection onto patterned ligands on surfaces exhibiting low non-specific adsorption rapidly yields the patterned protein surfaces. Fluorescence images after protein immobilization show high specificity of the target proteins to their respective surface patterned ligands. Time-of-flight secondary ion mass spectrometry (ToF-SIMS) imaging further supports the chemical specificity of streptavidin and HaloTag® for their surface patterned ligands from mixed protein solutions. However, ToF-SI

SUBMITTER: Grainger DW 

PROVIDER: S-EPMC3597123 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature