COLL 136 |
| Havazelet Bianco-Peled1, Ronit Biton2, Raymond Tu3, Yeshayahu Talmon1, and Matthew Tirrell3. (1) Department of Chemical Engineering, Technion - Israel Institute of Technology, Technion City, Haifa, 32000, Israel, (2) Inter-Departmental program for Biotechnology, Technion - Israel Institute of Technology, Technion City, Haifa, 32000, Israel, (3) Departments of Chemical Engineering and Materials, University of California, Santa Barbara, Santa Barbara, CA 93106 |
| Peptides amphiphile couple the specific functionality of proteins with the engineering convenience of synthetic amphiphiles. Theses molecules covalently link a peptide head-group, typically from active fragment of a larger protein, to hydrophobic alkyl tail. Our research is aimed at forming and characterizing covalently stabilized self-assembled peptide-amphiphiles aggregates that can be used as a platform for examination and design of biological systems. We have studied the self-assembly properties of a model DNA binding amphiphile, having a GCN4 peptide as the head group and polymerizble (methacrylic) group in the tail region, using a combination of cryo- transmission electron microscopy and small-angle x-ray scattering. Our results revealed a variety of self-assembled structures, ranging from simple geometries such as spherical or thread-like micelles to much less common geometries such as helical ribbons and tubules. Opposing common surfactants, the specific interaction between the head-groups seems to play an important role in determining the microstructure. |
|
Nanoscale Imaging of Biological Systems
Division of Colloid and Surface Chemistry |