Solid State NMR Methods Applied to Biomaterials

University Of Washington, Seattle WA

Investigators

Abstract

This project is aimed at developing characterization tools to be used to design self-assembling peptides that fold into defined a-helices or b-strands at polymeric biomaterial surfaces. The goal is to define peptide sequences that direct the assembly of functional peptides/proteins onto polymeric surfaces when the adaptors are fused to them. The project will develop an atomic level picture of the secondary structure and dynamics of peptides/proteins on biomaterial and nanoparticle surfaces and a high-resolution structural map of peptide-surface interactions. Recent studies of statherin peptides on hydroxyapatite crystals have demonstrated that there is sufficient sensitivity to perform similar solid state Nuclear Magnetic Resonance (ssNMR) characterization of peptides on a wider variety of surfaces. At the same time, NMR studies of peptide/protein conformation and dynamics on surfaces will be integrated with other spectroscopic-based surface characterization studies such as Near Edge X-ray Absorption Fine Structure (NEXAFS) and Time of Flight - Secondary Ion Mass Spectrometry (TOF-SIMS) to tie together new capabilities for the characterization of peptide conformation, orientation, and long-range order on biomaterial surfaces. The development of strategies for immobilizing functionally active proteins and peptides on polymeric surfaces is a central aspect of the biomaterials, tissue engineering, drug delivery, affinity separations, and diagnostic fields. These details are crucial to understanding why particular materials work well or don't work well, and the new molecular insights will provide important design criteria based on knowledge of peptide/protein structure, dynamics, and assembly at polymeric biomaterial surfaces. Students trained in this area of biomaterials science and applications will compete very well for both academic and industrial jobs. This project is jointly funded by the Division of Materials Research and the Chemistry Division.