IUVSTA 15th International Vacuum Congress (IVC-15), AVS 48th International Symposium (AVS-48), 11th International Conference on Solid Surfaces (ICSS-11)
    Biomaterials Monday Sessions
       Session BI-MoP

Paper BI-MoP12
Protein Template-Imprinting to Enhance Specific Protein Adsorption and Cell Adhesion

Monday, October 29, 2001, 5:30 pm, Room 134/135

Session: Biorecognition Poster Session
Presenter: J. Wang, University of Washington
Authors: J. Wang, University of Washington
X.H. Cheng, University of Washington
J. Schwartz, University of Washington
B.D. Ratner, University of Washington
Correspondent: Click to Email
Molecularly imprinted polymers (MIPs) are synthetic materials that possess specific recognition properties, and have found applications in enantiomer separation, enzyme mimics, and biomimetic biosensors. Among the common methods for molecular imprinting, the self-assembly approach is important for its resemblance to antibody-antigen, substrate-receptor, and enzyme-inhibitor interactions.@footnote 1@ The key for MIPs to perform recognition is that both the template and imprint are complementary in size, shape, and chemical functionality at the binding site. Nevertheless the self-assembly approach to molecular imprinting has been primarily done in organic solutions, and is less successful in directly imprinting larger biomolecules (proteins). Shi et al.@footnote 2@ developed an alternative approach to imprint protein molecules with disaccharide molecules and polymeric thin films. The protein imprints can preferentially recognize the original template protein, which is mainly attributed to cooperative non-covalent interactions including hydrogen bonds, hydrophobic interactions and van der Waals forces. We applied a similar imprint process with optimized conditions to create highly reproducible albumin (Alb) and fibronectin (FN) imprint surfaces. Surface analyses including ESCA, SIMS, and AFM were performed to characterize the variation in chemical composition after each imprint step. BAE cell adhesion studies demonstrated that the FN imprint surface could enhance cell attachment. Results from @super 125@I labeled binary protein competitive adsorption also showed that the FN imprint surface could preferentially adsorb higher amount of FN in a binary protein solution with Alb as the competing protein. @FootnoteText@ @footnote 1@Haupt, K. and Mosbach, K. Trends Biotechnol. (1998) 16: 468-475 @footnote 2@Shi, H., Tsai, W., Garrison, M., Ferrari, S. and Ratner, BD.. Nature. (1999) 398: 593-597.