Protein Crystal-Mediated Biotemplating

Abstract

Protein crystals, routinely prepared for the elucidation of protein 3-D structure by X-ray crystallography, present a highly accurate 3-D array of protein molecules. Along with the formation of this array, a complementary 3-D array of voids is also formed, with pattern, geometry, and size depending on the protein "building-block" and its packaging within the crystal. Here we present recent results demonstrating the feasibility of using the pores of protein crystals as a biotemplate for the preparation of composite materials. Our previously developed methods of monitoring the preservation of the 3-D protein crystal template throughout biotemplating of chemically cross-linked hydrogels and the elucidation of the mechanism of protein crystal cross-linking by glutaraldehyde were applied in this study to enable and demonstrate the feasibility of protein crystal-mediated biotemplating resulting in a 3-D array of silver particles located within the pores of the crystal. Our accumulated results indicate that the pool of protein crystals may be successfully exploited as a source of biotemplates for the fabrication of novel composite materials, in contrast to the common consideration of protein crystals as labile structures, useful only for the elucidation of the 3-D structure of proteins.