Templated biomineralization on self assembled protein fibers

ORAL

Abstract

We have previously shown that fibrillogenesis of extracellular matrix (ECM) proteins like Fibronectin and Elastin can be induced when adsorbed on charged polymer surfaces. These self assembled fiber networks reach sizes of dimensions similar to natural ECM. Here we present a study of biomineralization on these protein fibers, achieved using CaCO$_{3}$ through Kitano {\&} Flow cell methods. The mechanical properties were measured using$_{ }$Shear Modulation Force Microscopy (SMFM) as part of early stage mineralization studies. Results indicated increase in modulus with exposure time on fibers, with no increase off the fibers. Control studies with other Ca salts showed no change in fiber modulus, differentiating mineralization from salt adsorption. Late Stage Mineralization studied using ToF SIMS showed preferential Ca adsorption on the fibers. Optical Microscopy also showed preferential crystal formation on fibers. TEM was used to identity the crystal structure and orientation. Effect of proteins on crystal orientation and mineralization of natural ECM from osteoblasts are under study. Supported by USDOE Contract No DE-AC02-98CH10886, NSF-MRSEC {\&} BNL-SBU Seed Grant.

Authors

  • S. Palmaccio

    Sachem High School NY

  • K. Subburaman

  • N. Pernodet

    SUNY, Stony Brook Univ Stony Brook NY

  • S.-Y. Kwak

    Brookhaven National Laboratory

  • E. DiMasi

    Brookhaven National Laboratory, BNL, Upton, NY

  • S. Ge

    Stony Brook Univ Stony Brook NY

  • N.L. Yang

    CUNY, Staten Island, NY

  • M. Rafailovich

    SUNY, Dept. of Materials Science, SUNY at Stony Brook, Department of Materials Science, SUNY at Stony Brook, Dept. of Mat. Sci. and Engr,, State Univ. of New York at Stony Brook, Stony Brook Univ Stony Brook NY