TY - JOUR
T1 - Protein crystal-mediated biotemplating
AU - Cohen-Hadar, Noa
AU - Wine, Yariv
AU - Lagziel-Simis, Shira
AU - Moscovich-Dagan, Hila
AU - Dror, Yael
AU - Frolow, Felix
AU - Freeman, Amihay
PY - 2009
Y1 - 2009
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=59849114245&partnerID=8YFLogxK
U2 - 10.1615/JPorMedia.v12.i3.20
DO - 10.1615/JPorMedia.v12.i3.20
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AN - SCOPUS:59849114245
SN - 1091-028X
VL - 12
SP - 213
EP - 220
JO - Journal of Porous Media
JF - Journal of Porous Media
IS - 3
ER -