Inductively Heated Shape Memory Polymer for the Magnetic Actuation of Medical Devices

Submitted to IEEE Trans. Biomed. Eng.Presently there is interest in making medical devices such as expandable stents and intravascular microactuators from shape memory polymer (SMP). One of the key challenges in realizing SMP medical devices is the implementation of a safe and effective method of thermally actuating various device geometries in vivo. A novel scheme of actuation by Curie-thermoregulated inductive heating is presented. Prototype medical devices made from SMP loaded with Nickel Zinc ferrite ferromagnetic particles were actuated in air by applying an alternating magnetic field to induce heating. Dynamic mechanical thermal analysis was performed on both the particle-loaded and neat SMP materials to assess the impact of the ferrite particles on the mechanical properties of the samples. Calorimetry was used to quantify the rate of heat generation as a function of particle size and volumetric loading of ferrite particles in the SMP. These tests demonstrated the feasibility of SMP actuation by inductive heating. Rapid and uniform heating was achieved in complex device geometries and particle loading up to 10% volume content did not interfere with the shape recovery of the SMP.Lawrence Livermore National Lab

Force Spectroscopy of the Double-Tethered Concanavalin-A Mannose Bond

We present the measurement of the force required to rupture a single protein-sugar bond using a methodology that provides selective discrimination between specific and nonspecific binding events and helps verify the presence of a single functional molecule on the atomic force microscopy tip. In particular, the interaction force between a polymer-tethered concanavalin-A protein (ConA) and a similarly tethered mannose carbohydrate was measured as 47 ± 9 pN at a bond loading rate of ∼10 nN/s. Computer simulations of the polymer molecular configurations were used to determine the angles that the polymers could sweep out during binding and, in conjunction with mass spectrometry, used to separate the angular effects from the effects due to a distribution of tether lengths. We find that when using commercially available polymer tethers that vary in length from 19 to 29 nm, the angular effects are relatively small and the rupture distributions are dominated by the 10-nm width of the tether length distribution. In all, we show that tethering both a protein and its ligand allows for the determination of the single-molecule bond rupture force with high sensitivity and includes some validation for the presence of a single-tethered functional molecule on the atomic force microscopy tip