Abstract
Motor proteins are molecular machines that operate in living cells. These motor proteins have been used in vitro for applications such as nano- and microscale devices as transport systems in biosensors, biocomputing, and molecular communication. By introducing motor proteins into these devices, motor proteins become defective due to unfavorable binding to device surfaces, causing a decrease in transport speed or malfunctioning of transport. However, systematic experimental investigations of the effects of defective motors are hampered by difficulties in controlling the number of defective motors on surfaces. Here, we show a systematic study on the effects of defective motors on the motility of transport by using a mathematical model. The model predicted that motility is independent of the length of the associated filaments and depends on the ratio of the active motors. The model revealed that the ratio of active motors of more than 80% is required for sustainable motility. This insight would be useful in choosing appropriate materials for devices integrated with motor proteins.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Saper, G., Hess, H.: Synthetic systems powered by biological molecular motors. Chem. Rev. 120(1), 288–309 (2020)
Lin, C.T., Kao, M.T., Kurabayashi, K., Meyhofer, E.: Self-contained, biomolecular motor-driven protein sorting and concentrating in an ultrasensitive microfluidic chip. Nano Lett. 8(4), 1041–1046 (2008)
Fischer, T., Agarwal, A., Hess, H.: A smart dust biosensor powered by kinesin motors. Nat. Nanotechnol. 4(3), 162–166 (2009)
Lard, M., et al.: Ultrafast molecular motor driven nanoseparation and biosensing. Biosens. Bioelectron. 48, 145–152 (2013)
Nicolau, D.V., et al.: Parallel computation with molecular-motor-propelled agents in nanofabricated networks. Proc. Natl. Acad. Sci. USA 113(10), 2591–2596 (2016)
Farsad, N., Yilmaz, H.B., Eckford, A., Chae, C.-B., Guo, W.: A comprehensive survey of recent advancements in molecular communication. IEEE Commun. Surv. Tutorials 18(3), 1887–1919 (2014)
Nakano, T., Moore, M.J., Wei, F., Vasilakos, A.V., Shuai, J.: Molecular communication and networking: opportunities and challenges. IEEE Trans. Nanobiosci. 11(2), 135–148 (2012)
Bourdieu, L., Duke, T., Elowitz, M.B., Winkelmann, D.A., Leibler, S., Libchaber, A.: Spiral defects in motility assays: a measure of motor protein force. Phys. Rev. Lett. 75(1), 176–179 (1995)
Nitta, T., et al.: Comparing guiding track requirements for myosin- and kinesin-powered molecular shuttles. Nano Lett. 8(8), 2305–2309 (2008)
Rahman, M.A., Salhotra, A., Månsson, A.: Comparative analysis of widely used methods to remove nonfunctional myosin heads for the in vitro motility assay. J. Muscle Res. Cell Motil. 39(5–6), 175–187 (2019)
Hanson, K.L., et al.: Polymer surface properties control the function of heavy meromyosin in dynamic nanodevices. Biosens. Bioelectron. 93, 305–314 (2017)
Greenberg, M.J., Moore, J.R.: The molecular basis of frictional loads in the in vitro motility assay with applications to the study of the loaded mechanochemistry of molecular motors. Cytoskeleton 67(5), 273–285 (2010)
Kishino, A., Yanagida, T.: Force measurements by micromanipulation of a single actin filament by glass needles. Nature 334(6177), 74–76 (1988)
Riveline, D., et al.: Acting on actin: The electric motility assay. Eur. Biophys. J. 27(4), 403–408 (1998)
Nishizaka, T., Miyata, H., Yoshikawa, H., Ishiwata, S., Kinosita, K.: Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature 377(6546), 251–254 (1995)
Hill, A.V.: The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. London Ser. B Biol. Sci. 126(843), 136–195 (1938)
Ishigure, Y., Nitta, T.: Simulating an actomyosin in vitro motility assay: toward the rational design of actomyosin-based microtransporters. IEEE Trans. Nanobiosci. 14(6), 641–648 (2015)
Author information
Authors and Affiliations
Corresponding authors
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2021 ICST Institute for Computer Sciences, Social Informatics and Telecommunications Engineering
About this paper
Cite this paper
Kang’iri, S.M., Nitta, T. (2021). A Mathematical Model Predicting Gliding Speed of Actin Molecular Shuttles Over Myosin Motors in the Presence of Defective Motors. In: Nakano, T. (eds) Bio-Inspired Information and Communications Technologies. BICT 2021. Lecture Notes of the Institute for Computer Sciences, Social Informatics and Telecommunications Engineering, vol 403. Springer, Cham. https://doi.org/10.1007/978-3-030-92163-7_17
Download citation
DOI: https://doi.org/10.1007/978-3-030-92163-7_17
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-92162-0
Online ISBN: 978-3-030-92163-7
eBook Packages: Computer ScienceComputer Science (R0)