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Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins

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Proteins at surfaces and interfaces play important roles in the function and performance of materials in applications ranging from diagnostic assays to biomedical devices. To improve the performance of these materials, detailed molecular structure (conformation and orientation) along with the identity and concentrations of the surface-bound proteins on those materials must be determined. This article describes radiolabeling, surface plasmon resonance, quartz crystal microbalance with dissipation, X-ray photoelectron spectroscopy, secondary ion mass spectrometry, sum frequency generation spectroscopy, and computational techniques along with the information each technique provides for characterizing protein films. A multitechnique approach using both experimental and computation methods is required for these investigations. Although it is now possible to gain much insight into the structure of surface-bound proteins, it is still not possible to obtain the same level of structural detail about proteins on surfaces as can be obtained about proteins in crystals and solutions, especially for large, complex proteins. However, recent results have shown it is possible to obtain detailed structural information (e.g., backbone and side chain orientation) about small peptides (5-20 amino sequences) on surfaces. Current studies are extending these investigations to small proteins such as protein G B1 (~6 kDa). Approaches for furthering the capabilities for characterizing the molecular structure of surface-bound proteins are proposed.

TidsskriftAnnual Review of Analytical Chemistry
Sider (fra-til)389-412
Antal sider24
StatusUdgivet - jul. 2021

Bibliografisk note

Funding Information:
T.W. gratefully acknowledges the Novo Nordisk Foundation (NanoScat) and the European Research Council (ERC) F-BioIce Project 819039 for support of this work. D.G.C. gratefully acknowledges support from the US National Institutes of Health grant EB-002027 during the preparation of this manuscript

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