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Experimental Characterization of Peptide–Surface Interactions

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Bio-Inspired Nanotechnology

Abstract

Interactions between peptides and proteins with material surfaces are fundamental to a broad range of applications in biotechnology and biomedical engineering. Many different methods have been developed to measure a range of properties that quantify these types of interactions. In this chapter, three of these methods are presented for the determination of thermodynamic parameters that characterize peptide adsorption behavior, each of which is based on a different type of measurement. These three methods are surface plasmon resonance spectroscopy (SPR; spectroscopic-based method), atomic force microscopy (AFM; force-based method), and isothermal titration calorimetry (ITC; thermal-based method). The fundamental principles underlying each of these methods are presented followed by examples of their application for the determination of thermodynamic properties for specific peptide/protein-surface systems. The SPR method is presented for the determination of the standard-state adsorption free energy from adsorption isotherms characterizing the amount of peptide adsorbed as a function of solution concentration. This method, however, is limited to materials that can be used to form nanoscale-thick films about 100 nm thick or less on a gold biosensor substrate. For materials that are not easily formed into thin films, thus not being conducive for use with SPR, an AFM method is presented that can be used with any macroscopically flat surface through the correlation of peptide desorption force measured by AFM with adsorption free energy measurements by SPR. The third approach, ITC, measures thermal energy changes on adsorption with the method being applicable to the interaction of peptides/proteins with particles suspended in solution. The combined set of methods provides the means to quantitatively determine thermodynamic properties characterizing peptide and protein adsorption behavior for materials in either their bulk or particulate form, with important application to the broad range of technologies that involve contact between biological solutions and synthetic material surfaces.

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Acknowledgments

R.A. Latour and Y. Wei would like to acknowledge support for this research from the Defense Threat Reduction Agency-Joint Science and Technology Office for Chemical and Biological Defense (Grant no. HDTRA1-10-1-0028). The facilities used were also supported by NIH Grants 5P20RR021949-04 and 8P20GM103444-04. We also would like to thank Ms. Megan Grobman, Dr. Lara Gamble, and Dr. David Castner of NESAC/BIO at the University of Washington for assistance with surface characterization with XPS under the funding support by NIH NIBIB (grant # EB002027). C.C. Perry and M.J. Limo would like to thank their collaborators at the Air force office of scientific research (AFOSR) for funding and support of their studies (FA9550-10-1-0024 and FA9550-13-1-0040).

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Authors and Affiliations

  1. Interdisciplinary Biomedical Research Centre, Department of Chemistry and Forensic Science, School of Science and Technology, Nottingham Trent University, Clifton Lane, Nottingham, NG11 8NS, UK

    Marion J. Limo & Carole C. Perry

  2. Department of Bioengineering, 501 Rhodes Engineering Research Center, Clemson University, Clemson, SC, 29634, USA

    A. A. Thyparambil, Yang Wei & Robert A. Latour

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  1. Marion J. Limo
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  2. Carole C. Perry
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  3. A. A. Thyparambil
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  4. Yang Wei
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  5. Robert A. Latour
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Correspondence to Carole C. Perry .

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  1. Department of Chemistry, University of Miami, Coral Gables, Florida, USA

    Marc R. Knecht

  2. Institute for Frontier Materials, Deakin University, Geelong, Victoria, Australia

    Tiffany R. Walsh

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Limo, M.J., Perry, C.C., Thyparambil, A.A., Wei, Y., Latour, R.A. (2014). Experimental Characterization of Peptide–Surface Interactions. In: Knecht, M., Walsh, T. (eds) Bio-Inspired Nanotechnology. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-9446-1_3

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