Polymer surface properties control the function of heavy meromyosin in dynamic nanodevices.

Autor: Hanson KL; Industrial Research Institute Swinburne, Swinburne University of Technology, Hawthorn, Victoria, 3122 Australia., Fulga F; Department of Electrical Engineering and Electronics, The University of Liverpool, Liverpool, L693GJ United Kingdom., Dobroiu S; Department of Electrical Engineering and Electronics, The University of Liverpool, Liverpool, L693GJ United Kingdom., Solana G; Industrial Research Institute Swinburne, Swinburne University of Technology, Hawthorn, Victoria, 3122 Australia., Kaspar O; Department of Bioengineering, McGill University, Montreal, Quebec, H3A0C3 Canada., Tokarova V; Department of Bioengineering, McGill University, Montreal, Quebec, H3A0C3 Canada., Nicolau DV; Industrial Research Institute Swinburne, Swinburne University of Technology, Hawthorn, Victoria, 3122 Australia; Department of Electrical Engineering and Electronics, The University of Liverpool, Liverpool, L693GJ United Kingdom; Department of Bioengineering, McGill University, Montreal, Quebec, H3A0C3 Canada. Electronic address: dan.nicolau@mcgill.ca.
Jazyk: angličtina
Zdroj: Biosensors & bioelectronics [Biosens Bioelectron] 2017 Jul 15; Vol. 93, pp. 305-314. Date of Electronic Publication: 2016 Aug 20.
DOI: 10.1016/j.bios.2016.08.061
Abstrakt: The actin-myosin system, responsible for muscle contraction, is also the force-generating element in dynamic nanodevices operating with surface-immobilized motor proteins. These devices require materials that are amenable to micro- and nano-fabrication, but also preserve the bioactivity of molecular motors. The complexity of the protein-surface systems is greatly amplified by those of the polymer-fluid interface; and of the structure and function of molecular motors, making the study of these interactions critical to the success of molecular motor-based nanodevices. We measured the density of the adsorbed motor protein (heavy meromyosin, HMM) using quartz crystal microbalance; and motor bioactivity with ATPase assay, on a set of model surfaces, i.e., nitrocellulose, polystyrene, poly(methyl methacrylate), and poly(butyl methacrylate), poly(tert-butyl methacrylate). A higher hydrophobicity of the adsorbing material translates in a higher total number of HMM molecules per unit area, but also in a lower uptake of water, and a lower ratio of active per total HMM molecules per unit area. We also measured the motility characteristics of actin filaments on the model surfaces, i.e., velocity, smoothness and deflection of movement, determined via in vitro motility assays. The filament velocities were found to be controlled by the relative number of active HMM per total motors, rather than their absolute surface density. The study allowed the formulation of the general engineering principles for the selection of polymeric materials for the manufacturing of dynamic nanodevices using protein molecular motors.
(Copyright © 2016 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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