Remote Sensing of the Nano-Rheological Properties of Soft Materials Using Magnetic Nanoparticles and Magnetic AC Susceptometry.

We have developed a nano-rheological characterization tool to extract the frequency- and scale-dependent rheological properties of soft materials during oral processing. Taking advantage of AC susceptometry, the dynamic magnetization of magnetic nanoparticles blended in the matrix material is measured. The magnetic AC susceptibility spectra of the particles are affected by the viscosity and mechanical modulus of the matrix material and provide the rheological properties of the matrix. Commercially available iron-oxide magnetic nanoparticles with 80 and 100 nm particle sizes are used as tracers in the frequency range of 1 Hz-10 kHz. The AC susceptibility is measured using two differentially connected coils, and the effects of the sample temperature and distance with respect to the detection coils are investigated. The developed measurement setup shows the feasibility of remote nano-rheological measurements up to 2 cm from the coil system, which can be used to, e.g., monitor the texture of matrix materials during oral processing.

Mechanical properties of BiP protein determined by nano-rheology.

Immunoglobulin Binding Protein (BiP) is a chaperone and molecular motor belonging to the Hsp70 family, involved in the regulation of important biological processes such as synthesis, folding and translocation of proteins in the Endoplasmic Reticulum. BiP has two highly conserved domains: the N-terminal Nucleotide-Binding Domain (NBD), and the C-terminal Substrate-Binding Domain (SBD), connected by a hydrophobic linker. ATP binds and it is hydrolyzed to ADP in the NBD, and BiP's extended polypeptide substrates bind in the SBD. Like many molecular motors, BiP function depends on both structural and catalytic properties that may contribute to its performance. One novel approach to study the mechanical properties of BiP considers exploring the changes in the viscoelastic behavior upon ligand binding, using a technique called nano-rheology. This technique is essentially a traditional rheology experiment, in which an oscillatory force is directly applied to the protein under study, and the resulting average deformation is measured. Our results show that the folded state of the protein behaves like a viscoelastic material, getting softer when it binds nucleotides- ATP, ADP, and AMP-PNP-, but stiffer when binding HTFPAVL peptide substrate. Also, we observed that peptide binding dramatically increases the affinity for ADP, decreasing it dissociation constant (KD ) around 1000 times, demonstrating allosteric coupling between SBD and NBD domains.