|M.Sc Student||Bitton Ronit|
|Subject||Utilizing Peptide-Amphiphiles for the Preparation of Models|
of Biomimetic Systems
|Department||Department of Biotechnology||Supervisor||Professor Havazelet Bianco-Peled|
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 small-angle x-ray scattering and cryo- transmission electron microscopy. Our results revealed a variety of self-assembled structures. Moreover, opposing common surfactants, the specific interaction between the head-groups seems to play an important role in determining the microstructure. In aqueous solution, these peptide amphiphiles assembled into helical ribbons and tubules (hollow cylinders). The geometry of the self-assembled aggregate could be controlled by means of adding a co-surfactant. For example, addition of SDS induced formation spherical micelles, whereas adding Triton x-100 has lead to transition into thread-like micelles.