Formation, Hydration, and Structure of Biomolecules at the Protein-Surface Interface

University Of Texas At Austin, Austin TX

Investigators

Abstract

Proteins provide an extraordinary range of structures, properties, and functions that could be used in the design and building of novel devices and materials. Long term, this research has implications on the development of implantable medical devices including artificial joints and valves. Critical for such applications is for the protein to be effectively integrated into the devices. To this end, there is interest in attaching peptides and proteins to non-biological surfaces and materials reliably. The interface between the biomolecules and surface has properties are related to, but quite distinct from, those of the biological components and of the original surface. The three-dimensional structure and resulting function of proteins linked to surfaces can be radically different than in solution. Defining these differences is challenging. The research group of Dr. Lauren Webb at the University of Texas at Austin is addressing these challenges using a multidisciplinary research program focused on the investigation of biomolecules on rationally-designed and precisely-prepared surfaces. Dr. Webb fosters the participation of high school students in research in her own laboratories. Special emphasis is placed on increasing recruiting efforts in Texas high schools so that the diversity of students engaged in research reflects the diversity of the population of Texas. Despite the fact that the integration of biological molecules with non-biological materials is an area of current scientific interest, the understanding of the differences between the structures and properties of biomolecules attached to surfaces versus biomolecules in solution is relatively limited. Dr. Webb's research addresses the lack of fundamental understanding of what happens to biomolecules such as peptides and proteins in these alternative, substrate-bound environments. Dr. Webb's laboratory is using a unique chemical platform and an advanced set of analytical tools to address these fundamental questions from both an experimental and computational perspective. Gold surfaces are chemically functionalized with the electron-transfer protein azurin and studies of the protein's function are aimed at exploring conditions under which the gold remains stable. The research elucidates the mechanism of nucleation and formation of fibrils from surface-bound strand peptides. It also examines the influence of hydration of nominally dry surface-bound protein on the protein's structure and function. The experimental results are leveraged towards the development, testing, and validation of computational methods that may accurately predict the structure of proteins and peptides attached to artificial surfaces. Dr. Webb's long-term goal is to advance of the chemical understanding of peptides and protein behavior at surfaces so that the understanding reaches similar accuracy and predictability when compared to what is currently possible for solution-phase systems. This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.