The formation of complex macroscopic structures from component building blocks remains one of the most compelling problems in biology. This self ordering process lies at the heart of how a complex function, such as cell motility, can originate from a collection of structural and energy converting proteins. However, there are not yet a series of rules that predict the eventual structure or pattern formed by a self organization process from either mechanism. Only through a detailed understanding of the kinetics and energetics of the self-assembly/self organization sequence of model systems will it be possible to formulate such a set of rules. The research in this area will focus on the two dimensional organization of lipids and proteins at surfaces. Librairies of bi-and tri-polar lipids have been created and their self-assembly will be studied to construct structure-property phase diagrams to form the basis of a new rule set.
Phase Transition in Lipid Monolayers and Bilayers
The spatial organization of proteins, lipids, and guest molecules in lipid monolayers, membranes, and thin films ultimately determines their specific interactions and function. The spatial resolution of AFM and LFM (lateral force microscopy) has been used to investigate mixing in phospholipid monolayers and bilayers formed by Langmuir-Blodgett technique or by vesicle fusion onto mica. (Badia, Lafleur, Lennox)
Defects and Pore Formation in Membranes by Amphipathic Peptides
Organic design and synthesis is being used to access new materials that integrate the structural and functional characteristics of biopolymers with the stability and diversity of synthetic polymers. The principle aim of this research collaboration is to achieve an in-depth understanding of synthetic macrocycle and oligomer self-assembly within model membranes. In particular, the channel or pore-forming nature of synthetic foldamers and macrocycles are being studied using AFM.