This research focuses on studying amyloidogenic proteins associated with neurodegenerative diseases such as Alzheimer's disease (AD), prion encephalopathies, etc. These diseases are commonly classified as protein-misfolding or amyloid diseases due to their association with the rearrangement of specific proteins to non-native conformations which can promote aggregation and deposition.   We are especially interested in studying the physical/nanomechanical properties of lipid membranes, and how they modulate lipid-protein surface interactions and amyloid aggregation associated with neurodegenerative disease. The interaction of these proteins with various lipid surfaces has potential protein-misfolding disease implications. The results of this research can also provide valuable information on how protein deposits and biomolecules adhere and interact with various surface chemistries.  

This research focuses on studying the biochemical aspects of barnacle glue.  We are interested in using short bioinspired peptides and proteins to determine how barnacles use complex amyloid materials as strong and durable underwater adhesives. This led to the identification of new sequence patterning in the adhesive that dictates the assembly and displayed chemistry of sticky adhesive amyloid fibrils.  Amyloid materials are also used in nature via barnacle species by passively secreting a material that self-assembles into an ordered amyloid-like structure.  The amyloid-like permanent adhesive fabricated by the barnacle is an example of a class of proteins which use naturally occurring amyloid with a functional purpose.  Barnacle adhesive has become a desirable class of biomaterials in which to develop underwater adhesives inspired by the barnacle wet adhesive for the US Navy.  This project applies cutting-edge biomolecular and bioinformatic approaches to develop synthetic glue mimics.  This work is done in collaboration with the US Naval Research Laboratory in Washington, D.C.