Immobilization of Protein Molecules onto Homogeneous and Mixed Carboxylate-Terminated Self-Assembled Monolayers

• DOI: 10.1021/la970933h
• Publication Date: 2002-07-26T05:15:42Z
• Authors: Nikin Patel; Martyn C. Davies; Mark Hartshorne; Richard J. Heaton; Clive J. Roberts; Saul J. B. Tendler; Philip M. Williams
• Keywords: Biomolecule; Self-assembled monolayer; Carbodiimide; Protein Adsorption; Carboxylate

The attachment of biomolecules, in particular proteins, onto solid supports is fundamental the development advanced biosensors, bioreactors, affinity chromatographic separation materials, and many diagnostic techniques. In addition, effective investigation biomolecular structure function with scanning probe microscopy often requires a strong biomolecule to substrate. Here, we investigate binding protein catalase gold surfaces modified by self-assembled monolayers (SAMs). chemical physical adsorption molecules SAMs 3-mercaptopropanoic acid (3-MPA), 11-mercaptoundecanoic (11-MUA), mixture two thiols (mixed) was investigated utilizing tapping mode atomic force microscopy, tunneling surface plasmon resonance (SPR), static secondary ion mass spectrometry, X-ray photoelectron spectroscopy. concentration adsorbed on decreased following order: mixed > 11-MUA 3-MPA. Utilizing terminal carboxylic functionalities, immobilized water-soluble carbodiimide N-hydroxysuccinimide (NHS). Immobilization resulted increased coverage protein. SPR studies silver these indicate that immobilization NHS same order, namely