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Label-Free Measurement of Amyloid Elongation by Suspended Microchannel Resonators
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    Label-Free Measurement of Amyloid Elongation by Suspended Microchannel Resonators
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    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
    Third Institute of Physics, University of Goettingen, Friedrich-Hund-Platz 1, 37077 Göttingen, Germany
    § Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), 37073 Göttingen, Germany
    *E-mail: [email protected]. Fax: +49-551-2011577.
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    Analytical Chemistry

    Cite this: Anal. Chem. 2015, 87, 3, 1821–1828
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    https://doi.org/10.1021/ac503845f
    Published December 24, 2014
    Copyright © 2014 American Chemical Society

    Abstract

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    Protein aggregation is a widely studied phenomenon that is associated with many human diseases and with the degradation of biotechnological products. Here, we establish a new label-free method for characterizing the aggregation kinetics of proteins into amyloid fibrils by suspended microchannel resonators (SMR). SMR devices are unique in their ability to provide mass-based measurements under reaction-limited conditions in a 10 pL volume. To demonstrate the method, insulin seed fibrils of defined length, characterized by atomic force microscopy (AFM) and transmission electron microscopy (TEM), were covalently immobilized inside microchannels embedded within a micromechanical resonator, and the elongation of these fibrils under a continuous flow of monomer solution (rate ∼1 nL/s) was measured by monitoring the resonance frequency shift. The kinetics for concentrations below ∼0.6 mg/mL fits well with an irreversible bimolecular binding model with the rate constant kon = (1.2 ± 0.1) × 103 M–1 s–1. Rate saturation occurred at higher concentrations. The nonlinear on-rate for monomer concentrations from 0 to 6 mg/mL and for temperatures from 20 to 42 °C fit well globally with an energy landscape model characterized by a single activation barrier. Finally, elongation rates were studied under different solution conditions and in the presence of a small molecule inhibitor of amyloid growth. Due to the low volume requirements, high precision, and speed of SMR measurements, the method may become a valuable new tool in the screening for inhibitors and the study of fundamental biophysical mechanisms of protein aggregation processes.

    Copyright © 2014 American Chemical Society

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    Supporting Information

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    Sensitivity calibration of the SMR device, electron micrographs of prepared seed fibrils, and solubility test of insulin monomers. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cited By

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    This article is cited by 12 publications.

    1. Wen Wang, Jiaxing Zhang, Wei Qi, Rongxin Su, Zhimin He, Xin Peng. Alizarin and Purpurin from Rubia tinctorum L. Suppress Insulin Fibrillation and Reduce the Amyloid-Induced Cytotoxicity. ACS Chemical Neuroscience 2021, 12 (12) , 2182-2193. https://doi.org/10.1021/acschemneuro.1c00177
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    9. Manizhe Zakeri, Seyed Mahmoud Seyedi Sahebari. Modeling and simulation of a suspended microchannel resonator nano-sensor. Microsystem Technologies 2018, 24 (2) , 1153-1166. https://doi.org/10.1007/s00542-017-3478-6
    10. Han Yan, Wen-Ming Zhang, Hui-Ming Jiang, Kai-Ming Hu. Pull-In Effect of Suspended Microchannel Resonator Sensor Subjected to Electrostatic Actuation. Sensors 2017, 17 (12) , 114. https://doi.org/10.3390/s17010114
    11. Han Yan, Wen-Ming Zhang, Hui-Ming Jiang, Kai-Ming Hu, Fang-Jun Hong, Zhi-Ke Peng, Guang Meng. A measurement criterion for accurate mass detection using vibrating suspended microchannel resonators. Journal of Sound and Vibration 2017, 403 , 1-20. https://doi.org/10.1016/j.jsv.2017.05.030
    12. Wen-Ming Zhang, Han Yan, Hui-Ming Jiang, Kai-Ming Hu, Zhi-Ke Peng, Guang Meng. Dynamics of suspended microchannel resonators conveying opposite internal fluid flow: Stability, frequency shift and energy dissipation. Journal of Sound and Vibration 2016, 368 , 103-120. https://doi.org/10.1016/j.jsv.2016.01.029

    Analytical Chemistry

    Cite this: Anal. Chem. 2015, 87, 3, 1821–1828
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ac503845f
    Published December 24, 2014
    Copyright © 2014 American Chemical Society

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