(734i) Protein Confinement in Mesoporous Materials

Challenges in biotechnology and therapeutics have brought considerable interest to protein immobilization in porous hosts¹.  Hence, it is necessary to develop a more thorough understanding of the fundamental behavior of protein confinement.  While pore surface properties such as charge and hydrophobicity are known to dramatically affect protein stability², our previous studies on confinement effects in nanoporous particles have shown that geometric properties such as surface curvature play a significant role as well³.  These studies have shown that high concave surface curvature can stabilize the native protein structure and protect enzymes from extreme environmental conditions.  Here we expand our investigation to include additional confinement geometries including the Ia3d (KIT-6), Im3m (SBA-16), and Fm3m (FDU-12) cubic space groups while maintaining consistent surface properties.  This allows for further elucidation of the fundamental dependence of protein behavior on protein confinement geometry.

References:

1. Siefker J, Karande P, Coppens M-O. Packaging Biological Cargoes in Mesoporous Materials: Opportunities for Drug Delivery. Expert Opin Drug Deliv. 2014 (submitted)
2. Yuan L, Yu Q, Li D, Chen H. Surface Modification to Control Protein/Surface Interactions. Macromolecular Bioscience. 2011;11(8):1031
3. Sang L-C, Coppens M-O. Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores. Phys Chem Chem Phys. 2011;13(14):6689