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Molecular-Scale Studies of Proteins at Model Biomaterial Surfaces by Atomic Force Microscopy

Published online by Cambridge University Press:  02 July 2020

Christopher A. Siedlecki*
Affiliation:
The Pennsylvania State University Departments of Surgery and Bioengineering, College of Medicine, Hershey, PA, 17033
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Abstract

A widely accepted tenet of biomaterials research is that the initial step following contact of a synthetic material with blood is the rapid adsorption of plasma proteins. The composition of this adsorbed protein layer is dependent on a variety of factors, including the surface properties of the implant material and the nature of the adsorbing proteins, and the composition and function of this protein layer is important in the subsequent biological response and ultimately the success or failure of the implanted material. While a great amount of effort has gone into developing structure/function responses for implanted biomaterials, there is still much about the molecular level interactions to be determined. We utilized atomic force microscopy (AFM) to investigate the molecular-level interactions of proteins with model biomaterial substrates. The AFM is unique in that it offers the opportunity to characterize interfacial environments, determine material properties, measure protein/surface interaction forces, and visualize the tertiary structure of adsorbed proteins.

Type
Advances in Imaging Techniques for Biomaterlals (Organized by S. Eppel)
Copyright
Copyright © Microscopy Society of America 2001

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References

references

1.Garrett, J. T., Siedlecki, C. A., and Runt., J. Microdomain morphology of poly(urethane urea) multiblock copolymers. Macromolecules, (Submitted).Google Scholar
2. The PUU films were provided by Dr.Jim Runt, and James, Garrett from The Pennsylvania State University. The Whitaker Foundation provided funding for these studies.Google Scholar