Exploration of Small Peptide Binding Interactions with Inorganic Surfaces Across Timescales

Peptide adhesion presents a novel method of binding surfaces which could not otherwise be permanently bound through conventional methods. Two such surfaces of practical interest are titanium dioxide (the surface of osseous implants) and hydroxyapatite (the primary mineral component of bone). The work described in this thesis strives to ascertain whether or not peptide adhesion could provide a more reliable bond between these through surfaces. In order to answer this question, research within this volume is performed to understand what features of peptides make them amenable to certain surfaces. In this work, two peptides are studied to determine their mode of selective binding to these surfaces. Titanium Binding Peptide (TBP) is investigated for its ability to bind to various surfaces through binding isotherms, and its mode of binding is interrogated through mutation studies, solid state NMR, DEST, NOSEY, and STD-NMR experiments. Likewise, the α-1 fragment of osteocalcin was investigated via binding isotherms for its ability to bind to both hydroxyapatite and titania, and its method of binding to the later was studied through solid state NMR in order to determine a free and bound structure. From these structures, we used our chemical intuition to deduce a likely candidate for a binding motif.

Author dc:creator

• Gebhart, Rachel Nicole

Advisor dc:contributor.advisor

• Drobny, Gary P

• Biomineral Interface
• Nuclear Magnetic Resonance
• Solid State NMR
• Spectroscopy
• Physical chemistry
• Biochemistry
• Chemistry

Statement dc:rights

• none

Language dc:language.iso

en_US

Handle dc:identifier.uri

http://hdl.handle.net/1773/46749

OAI identifier oai:identifier

oai:digital.lib.washington.edu:1773/46749