NESAC/BIO provides the biomedical research community with state-of- the art surface analysis expertise, instrumentation, experimental protocols, and data analysis methods to address biological and medical problems involving the surface and interfacial regions. Since the nature of the surface strongly influences the composition and recognizability of the adsorbed protein layer and the subsequent cellular interactions, understanding the structure of surfaces and the nature of adsorbed protein films are key links in understanding interfacial biology. ESCA, static SIMS, and SPM provide a powerful set of set of complementary techniques for addressing the challenges and complexity of the new generation of biomaterials being developed with molecular recognition principles.
The specific aims of the Technological Research and development projects are: 1) Surface Analysis Standards for Technique Development, 2) Chemical State Imaging Technique Development and, and 3) Characterization of Proteins at Surfaces and Interfaces. Over the next five years the focus of NESAC/BIO will expand from spectroscopic analysis to include image analysis. Multivariate analysis methods will be developed to enhance our ability to obtain chemical state images at high spatial resolution. Standards used in the development of these techniques will include self-assembled monolayers, peptides, and ordered proteins.
The specific aim of the Collaborative research projects is to use the surface analysis techniques and methods developed in the TRD projects to address important biomedical research problems. The areas of investigation include biosensors, tissue engineering, self-assembled films, biomineralization, cell growth surfaces with peptides, antibacterial polyurethane surfaces, novel surfactants for controlling biomolecule adhesion, coated vascular stents, and biomaterials with specific recognition sites. NESAC/BIO Service activities will focus on the development and optimization of biomedical devices. Current biomedical device service projects include cochlear implants, glucose sensors, and coated guidewires. Dissemination efforts will focus on scientific publications, presentations at scientific meetings, a yearly newsletter, booths a key national meetings, and the NESAC/BIO Website. Training projects will include a three-day short course offered at the University of Washington each year on biomedical surface analysis along with one-on- one instrument and data analysis training.
|Tyler, Bonnie J; Peterson, Richard E (2013) Dead-time correction for time-of-flight secondary-ion mass spectral images: a critical issue in multivariate image analysis. Surf Interface Anal 45:475-478|
|Tyler, B J; Bruening, C; Rangaranjan, S et al. (2011) TOF-SIMS imaging of adsorbed proteins on topographically complex surfaces with Bi(3) (+) primary ions. Biointerphases 6:135|
|Medzihradszky, Katalin F (2008) Characterization of site-specific N-glycosylation. Methods Mol Biol 446:293-316|
|Medzihradszky, Katalin F (2005) Peptide sequence analysis. Methods Enzymol 402:209-44|
|Sanders, Joan E; Lamont, Sarah E; Karchin, Ari et al. (2005) Fibro-porous meshes made from polyurethane micro-fibers: effects of surface charge on tissue response. Biomaterials 26:813-8|
|Medzihradszky, Katalin F (2005) In-solution digestion of proteins for mass spectrometry. Methods Enzymol 405:50-65|
|Medzihradszky, Katalin F (2005) Characterization of protein N-glycosylation. Methods Enzymol 405:116-38|
|Wagner, Victoria E; Koberstein, Jeffrey T; Bryers, James D (2004) Protein and bacterial fouling characteristics of peptide and antibody decorated surfaces of PEG-poly(acrylic acid) co-polymers. Biomaterials 25:2247-63|
|Tsai, W B; Shi, Q; Grunkemeier, J M et al. (2004) Platelet adhesion to radiofrequency glow-discharge-deposited fluorocarbon polymers preadsorbed with selectively depleted plasmas show the primary role of fibrinogen. J Biomater Sci Polym Ed 15:817-40|
|Martin, Stephanie M; Schwartz, Jeffrey L; Giachelli, Cecilia M et al. (2004) Enhancing the biological activity of immobilized osteopontin using a type-1 collagen affinity coating. J Biomed Mater Res A 70:10-9|
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