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Updated: Aug 29, 2025

Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
Characterizing protein-surface and protein-nanoparticle conjugates: Activity, binding, and structure
Joshua M Correira1, Paul R Handali1, Lauren J Webb1
1Department of Chemistry, Texas Materials Institute, and Interdisciplinary Life Sciences Program, The University of Texas at Austin, 105 E 24th St. STOP A5300, Austin, Texas 78712-1224, USA.
Abstract:
Many sensors and catalysts composed of proteins immobilized on inorganic materials have been reported over the past few decades. Despite some examples of functional protein-surface and protein-nanoparticle conjugates, thorough characterization of the biological-abiological interface at the heart of these materials and devices is often overlooked in lieu of demonstrating acceptable system performance. This has resulted in a focus on generating functioning protein-based devices without a concerted effort to develop reliable tools necessary to measure the fundamental properties of the bio-abio interface, such as surface concentration, biomolecular structure, and activity. In this Perspective, we discuss current methods used to characterize these critical properties of devices that operate by integrating a protein into both flat surfaces and nanoparticle materials. We highlight the advantages and drawbacks of each method as they relate to understanding the function of the protein-surface interface and explore the manner in which an informed understanding of this complex interaction leads directly to the advancement of protein-based materials and technology.
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