AVS 51st International Symposium
    Biomaterial Interfaces Monday Sessions
       Session BI-MoM

Invited Paper BI-MoM1
High-Resolution Structural and Dynamic Characterization of Proteins on Biomaterial Surfaces

Monday, November 15, 2004, 8:20 am, Room 210D

Session: In-Situ Spectroscopy of Biomolecules at Interface
Presenter: P.S. Stayton, University of Washington
Authors: P.S. Stayton, University of Washington
G.P. Drobny, University of Washington
Correspondent: Click to Email
The development of materials with bioactive interfaces is a major focus of the biomaterials and tissue engineering communities. There is also considerable interest in the immobilization of active peptides and proteins in separations, diagnostics, proteomics, and cell culture technologies. In order to design appropriate biomaterial modification strategies where activity is retained, it is desirable to elucidate how protein structure, dynamics and orientation are related to the biomaterial surface properties and immobilization chemistries. Solid-state NMR techniques provide an opportunity to determine these molecular structure and dynamics properties of proteins and peptides on many different types of biomaterial surfaces. In particular, the high-resolution backbone conformation of proteins can be determined, the binding "footprint" - or which amino acid side-chains actually contact the surface can be determined, the role of water at the protein-material interface can be investigated, the dynamics of specific protein side-chains can be determined, and the orientation of the protein on the crystal surface can be determined. Homonuclear and heteronuclear dipolar recoupling solid-state NMR techniques, combined with dynamic studies, have been applied to determine the structure, dynamics and orientation of proteins and peptides immobilized on polymeric biomaterial surfaces, surface-modified nanoparticles, and on inorganic crystals such as hydroxyapatite.