(324d) Investigating Antibody Access to Adsorbed Protein Nanocapsule Interiors Using the Quartz Crystal Microbalance and Surface Plasmon Resonance

Vaults are hollow, ribonucleoprotein capsules (72.5 x 41 x 41 nm) comprised primarily of 96 self-assembled copies of one 97 kDa protein. Vaults have been found to open into halves when deposited on positively charged surfaces. The biological function for these nanocapsules, which are ubiquitous intracellular components of eukaryotes, is unknown; yet they may prove useful for material entrapment and drug delivery. Our aim is to design mechanisms for reversible vault assembly/disassembly in order to control the encapsulation and release of materials. We have previously shown that vaults disassemble into halves when exposed to pH values below pH 4.0. Current studies investigate molecular access to the interiors of vaults that have been adsorbed onto modified quartz crystal microbalance (QCM) and surface plasmon resonance (SPR) substrates, and opened by exposure to low pH. We have employed the use of antibodies which have specific affinity for peptide tags internalized within the vault waist in effort to demonstrate targeted material encapsulation within vaults, thereby exploiting their use as nanocarriers. All vault components have been cloned and overexpressed, thereby providing an attractive system for the study of biological self-assembly and a potentially versatile platform for biomaterials design.