Macromolecular Scaffolds for Immobilizing Small Molecule Microarrays in Label-Free Detection of Protein−Ligand Interactions on Solid Support

We explored two macromolecular scaffolds, bovine serum albumin (BSA) and polyvinyl alcohol (PVA), as chemically complementary platforms for immobilizing small molecule compounds on functionalized glass slides. We conjugated biotin molecules to BSA and amine-derivatized PVA and subsequently immobiliz...

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Bibliographic Details
Published in:Analytical chemistry (Washington) 2009-07, Vol.81 (13), p.5373-5380
Main Authors: Sun, Y. S, Landry, J. P, Fei, Y. Y, Zhu, X. D, Luo, J. T, Wang, X. B, Lam, K. S
Format: Article
Language:English
Subjects:
Analytical chemistry
Animals
Biotin - chemistry
Biotin - immunology
Cattle
Chemistry
Exact sciences and technology
General, instrumentation
Glass
Immunoglobulin Fab Fragments - chemistry
Immunoglobulin Fab Fragments - immunology
Kinetics
Ligands
Molecular chemistry
Polyvinyl alcohol
Polyvinyl Alcohol - chemistry
Protein Array Analysis - methods
Protein Binding
Proteins
Serum Albumin, Bovine - chemistry
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Summary:We explored two macromolecular scaffolds, bovine serum albumin (BSA) and polyvinyl alcohol (PVA), as chemically complementary platforms for immobilizing small molecule compounds on functionalized glass slides. We conjugated biotin molecules to BSA and amine-derivatized PVA and subsequently immobilized the conjugates on epoxy-functionalized glass slides through reaction of free amine residues on BSA and PVA with surface-bound epoxy groups. We studied binding reactions of such immobilized small molecule targets with solution-phase protein probes using an oblique-incidence reflectivity difference scanning optical microscope. The results showed that both BSA and amine-derivatized PVA were effective and efficient as carriers of small molecules with NHS residues and fluoric residues and for immobilization on epoxy-coated solid surfaces. A significant fraction of the conjugated small molecules retain their innate chemical activity.
ISSN:0003-2700
1520-6882
DOI:10.1021/ac900889p