Structure and Function of Membrane-Associated Peptides and Proteins

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Every cell is enveloped by a membrane, as are the various compartments within it. Therefore most biological processes either occur at or require transit through a membrane. Indeed, ca. 33% of all proteins are membrane associated. Despite their importance, however, relatively little is known about the 3D architecture of membrane proteins. Knowledge of protein structure is needed to understand function. The goal of our research is to study the interplay between protein structure and function in biological membranes. Despite the many challenges associated with working with membrane proteins (e.g. producing large amounts, limitations of the methods, etc.), we have made great strides in this area by studying biologically & pharmaceutically important biomolecules in their native lipid environment. We investigate 4 classes of proteins in biologically relevant lipids, using a wide range of biophysical methods: 1) ANTIMICROBIAL PEPTIDES: The rise of highly resistant "superbugs" imposes significant health and economic costs throughout the world. We are developing new sustainable antibiotics, by investigating the mechanisms of action of different types of bactericidal agents, both as free compounds and in implants. 2) VIRAL PROTEINS: Human Herpes Virus type 6 (HHV6) and type 7 (HHV7) are two viruses that have been found to be associated with Multiple Sclerosis (MS) and immunodeficiency-related diseases. We study the U24 membrane protein to determine how it may be linked to MS by tricking the body into attacking itself. 3) PHAGE COAT PROTEINS: How biological macromolecules insert into membranes in order to form large assemblies and to carry out highly specific functions is very poorly understood. We study the structure of filamentous bacteriophage proteins and their association to learn about these fundamental processes. 4) FUSION PEPTIDES: Viral fusion proteins contain short segments named fusion peptides (FP), which play a vital role in the entry of viruses into cells. We work on FPs from viruses related to West Nile Virus to determine how the structure relates to viral entry.