COLL 44 |
| Christopher M. Yip, Department of Chemical Engineering and Applied Chemistry / Institute of Biomaterials and Biomedical Engineering, Department of Chemical Engineering and Applied Chemistry / Institute of Biomaterials and Biomedical Engineering, University of Toronto, 407 - 4 Taddle Creek Rd, Toronto, ON M5S3G9 |
| The rational design of protein-based supramolecular architectures requires careful consideration of both intramolecular structure and the intermolecular interactions that control their self-association into higher order structures. We are particularly interested in the role of interfacial structure and chemistry in defining the nucleation and growth of these systems and specifically the synthesis of extended two-dimensional structures. While our previous investigations of protein crystal growth provided intriguing insights into the mechanisms of self-assembly into the solid-state, our recent efforts have focused more on the role of heterogeneous two-dimensional interfaces – from membrane surfaces to crystalline substrates – in directing the self-assembly of proteins. In particular, we have used extended-duration correlated atomic force microscopy techniques to investigate the role of electrostatic and hydrophobic forces on the assembly of several model ß-helix and ß-sheet forming peptides. Our results combined with molecular modeling suggest that careful manipulation of surface electrostatics and hydrophobics can be used to control protein assembly at interfaces. |
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Nanoscale Imaging of Biological Systems
Division of Colloid and Surface Chemistry |