(162d) Protein Analogous Micelles

Peptides are functional modules of protein macromolecules that can be displayed apart from the whole protein to create biofunctional surfaces and interfaces, or can be re-assembled in new ways to create synthetic mimics of protein structures. Each of these routes are being employed to gain new insight into protein folding and to develop new, functional, biomolecular materials. Examples of work from our laboratory in this area using peptide-lipid conjugate molecules (peptide amphiphiles) will be discussed relating to multi-functional interfaces, DNA-binding peptide assemblies, and protein analogous micelles for cancer and cardiovascular therapeutics. This work has been pursued in collaboration with numerous people at the University of Minnesota, UC Santa Barbara and UC Berkeley, including: Gregg Fields, Erkki Ruoslahti, Frank Bates, Ishi Talmon, Peter Berndt, Efie Kokkoli, Angie Dillow, Havazelet Bianco-Peled, Shiv Chiruvolu, Markus Biesalski, Jim Schneider, Yoav Dori, Sanjay Kumar, Kraig Haverstick, Sarah Ochsenhirt, Tushar Gore, Teika Pakalns, Ray Tu, Alex Chu-Kung, Nathan Lockwood, Dimitris Stroumpoulis, Tomoko Shimada,  Mark Kastantin, Badri Ananthanarayanan, Dimitris Missirlis, Won Huh, Matt Kade, Matt Black, Rachel Marullo, Katie Megley, Amanda Trent, Dan Krogstad and Laurie Drews.