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Anal Bioanal Chem

Title:Antibody orientation enhanced by selective polymer-protein noncovalent interactions
Author(s):Clarizia, L. J. Sok, D. Wei, M. Mead, J. Barry, C. McDonald, M. J.
Address:Department of Chemistry, University of Massachusetts, Lowell, MA, 01854, USA.
Year:2009 Mar
Journal Title:Anal Bioanal Chem
Page Number:1531-8
ISSN/ISBN:1618-2650 (Electronic)
Abstract:A unique interaction has been found between protein G' (a truncated recombinant bacterial "alphabet" protein which aligns by noncovalent attachment to the antibody stem) and poly(methyl methacrylate), a thermoplastic polymer substrate, which can be easily fabricated using high-rate processes. Significantly improved orientation efficiency with traditional passive adsorption for this system (termed ALYGNSA) has been achieved as compared to the same assay performed on a polystyrene substrate with protein G'. Results were consistent with an average alignment of 80% of the human immunoglobulin G capture antibody which translated into a 30% to 50% improved alignment over an array of industry standards tested. Laser scanning confocal microscopy confirmed the immunological results. Studies of additional poly(methyl methacrylate) polymer derivatives and protein biolinker (A and AG) combinations have been conducted and have revealed different degrees of antibody alignment. These findings may lead to additional novel noncovalent methods of antibody orientation and greater sensitivity in immunological assays.

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Citation: El-Sayed AM. The Pherobase: Database of Pheromones and Semiochemicals. <>.
The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.