27 research outputs found

    Torque on magnetic particles for biomedical applications

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    Torque on magnetic particles for biomedical applications

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    Dynamics and thermodynamics of decay in charged clusters

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    We propose a method for quantifying charge-driven instabilities in clusters, based on equilibrium simulations under confinement at constant external pressure. This approach makes no assumptions about the mode of decay and allows different clusters to be compared on an equal footing. A comprehensive survey of stability in model clusters of 309 Lennard-Jones particles augmented with Coulomb interactions is presented. We proceed to examine dynamic signatures of instability, finding that rate constants for ejection of charged particles increase smoothly as a function of total charge with no sudden changes. For clusters where many particles carry charge, ejection of individual charges competes with a fission process that leads to more symmetric division of the cluster into large fragments. The rate constants for fission depend much more sensitively on total charge than those for ejection of individual particles

    Dipolar-coupled moment correlations in clusters of magnetic nanoparticles

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    Here, we investigate the nature of the moment coupling between 10-nm DMSA-coated magnetic nanoparticles, in both colloidal dispersion and in powder form. The individual iron oxide cores were composed of > 95% maghemite and agglomerated to clusters. At room temperature the ensemble behaved as a superparamagnet according to M\"ossbauer and magnetization measurements, however, with clear signs of dipolar interactions at low temperatures. Analysis of temperature-dependent AC susceptibility data in the superparamagnetic regime indicates a tendency for dipolar coupled anticorrelations of the core moments within the clusters. To resolve the directional correlations between the particle moments we performed polarized small-angle neutron scattering and determined the magnetic spin-flip cross-section of the powder in low magnetic field at 300 K. We extract the underlying pair distance distribution function of the magnetization vector field by an indirect Fourier transform of the cross-section, and which suggests positive as well as negative correlations between nearest neighbor moments, with anticorrelations clearly dominating for next-nearest moments. These tendencies are confirmed by Monte Carlo simulations of such core-clusters.Comment: 11 pages, 6 figure

    Torque on magnetic particles for biomedical applications

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    Conformation switching of single native proteins revealed by nanomechanical probing without a pulling force

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    Protein conformational changes are essential to biological function, and the heterogeneous nature of the corresponding protein states provokes an interest to measure conformational changes at the single molecule level. Here we demonstrate that conformational changes in single native proteins can be revealed by non-covalent antibody-targeting of specific domains within the protein, using nanomechanical probing without an applied pulling force. The protein of interest was captured between a particle and a substrate and three properties were quantified: the twist amplitude related to an applied torque, torsional compliance related to rotational Brownian motion, and translational Brownian displacement. Calcium-dependent conformation switching was studied in native human cardiac troponin, a heterotrimer protein complex that regulates the contraction and relaxation of heart muscle cells and is also a key biomarker for diagnosing myocardial infarction. The data reveal a change in mechanical properties upon conformation switching from the non-saturated to the calcium-saturated state, which in cardiomyocytes gives myosin motor proteins access to actin filaments. A clear increase was observed in the molecular stiffness for the calcium-saturated protein conformation. Using libraries of monoclonal antibodies, the nanomechanical probing of conformation by antibody targeting opens avenues for characterizing single native protein complexes for research as well as for diagnostic applications

    Rotating magnetic particles for lab-on-chip applications-a comprehensive review

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    \u3cp\u3eMagnetic particles are widely used in lab-on-chip and biosensing applications, because they have a high surface-to-volume ratio, they can be actuated with magnetic fields and many biofunctionalization options are available. The most well-known actuation method is to apply a magnetic field gradient which generates a translational force on the particles and allows separation of the particles from a suspension. A more recently developed magnetic actuation method is to exert torque on magnetic particles by a rotating magnetic field. Rotational actuation can be achieved with a field that is uniform in space and it allows for a precise control of torque, orientation, and angular velocity of magnetic particles in lab-on-chip devices. A wide range of studies have been performed with rotating MPs, demonstrating fluid mixing, concentration determination of biological molecules in solution, and characterization of structure and function of biomolecules at the single-molecule level. In this paper we give a comprehensive review of the historical development of MP rotation studies, including configurations for field generation, physical model descriptions, and biological applications. We conclude by sketching the scientific and technological developments that can be expected in the future in the field of rotating magnetic particles for lab-on-chip applications.\u3c/p\u3
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