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Updated: Jul 7, 2026

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
Published on: August 20, 2018
Functionalization of AlN surface and effect of spacer density on Escherichia coli pili-antibody molecular recognition
Ting Cao1, Anfeng Wang, Xuemei Liang
1Department of Chemical Engineering and Materials Science, Wayne State University, 5050 Anthony Wayne Drive, Detroit, MI 48202, USA.
Abstract:
The immobilization of antibodies to sensor surfaces is critical in biochemical sensor development. In this study, Jeffamine spacers were employed to tether Escherichia coli K99 pilus antibody to AlN/sapphire surfaces which may allow the antibody to freely reorient and potentially improving the antigen capture efficiency. Spacer density was one of the key parameters to be optimized in studying its effect on the immobilization of antibody. The spacer density was controlled by functionalizing AlN/sapphire surfaces with a mixed (3-glycidyloxypropyl)trimethoxysilane (GPTMS) and trichloro(1H,1H,2H,2H-perfluoroctyl)silane (FAS) self-assembled monolayer (SAM) through a step-wise method. Contact angle measurement and X-ray photoelectron spectroscopy (XPS) were used to characterize the surface coverage of GPTMS and surface chemical composition. Compared to spacer fully covered samples, the capture efficiency was improved by approximately 28% with optimal Jeffamine ED 600 spacer density, which depends on the spacer properties such as the number of monomer units and its size.

