The classification and therapeutic applications of molecular motors

Li, Mingyuan; Li, Yuan; Jia, Lin; Li, Shiqin; Li, Meng; Yang, Guang; Liu, Nan; Ren, Hongmeng; Mou, Mingqi; Zheng, Aiping; Hua, Sun

doi:10.1016/j.ejmcr.2021.100009

Cited by 4 publications

(3 citation statements)

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“…Molecular motors are nanomachines that convert chemical energy or light into motion. Natural molecular motors are usually protein or RNA assemblies [ 1 , 2 , 3 , 4 ]. Their roles include the transportation of intracellular substances, motion, mitosis, separating DNA strands, and the construction of the cytoskeleton.…”

Section: Introductionmentioning

confidence: 99%

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Long-Time Dynamics of Selected Molecular-Motor Components Using a Physics-Based Coarse-Grained Approach

et al. 2023

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Molecular motors are essential for the movement and transportation of macromolecules in living organisms. Among them, rotatory motors are particularly efficient. In this study, we investigated the long-term dynamics of the designed left-handed alpha/alpha toroid (PDB: 4YY2), the RBM2 flagellum protein ring from Salmonella (PDB: 6SD5), and the V-type Na+-ATPase rotor in Enterococcus hirae (PDB: 2BL2) using microcanonical and canonical molecular dynamics simulations with the coarse-grained UNRES force field, including a lipid-membrane model, on a millisecond laboratory time scale. Our results demonstrate that rotational motion can occur with zero total angular momentum in the microcanonical regime and that thermal motions can be converted into net rotation in the canonical regime, as previously observed in simulations of smaller cyclic molecules. For 6SD5 and 2BL2, net rotation (with a ratcheting pattern) occurring only about the pivot of the respective system was observed in canonical simulations. The extent and direction of the rotation depended on the initial conditions. This result suggests that rotatory molecular motors can convert thermal oscillations into net rotational motion. The energy from ATP hydrolysis is required probably to set the direction and extent of rotation. Our findings highlight the importance of molecular-motor structures in facilitating movement and transportation within living organisms.

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Section: Introductionmentioning

confidence: 99%

“…Molecular motors are powered by ATP hydrolysis [ 1 , 2 , 3 , 4 ]. However, the process of energy conversion differs from that of macroscale engines because of its stochastic nature [ 3 , 11 , 13 , 14 ].…”

Section: Introductionmentioning

confidence: 99%

Long-Time Dynamics of Selected Molecular-Motor Components Using a Physics-Based Coarse-Grained Approach

et al. 2023

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“…[1][2][3][4][5][6] Their transport abilities could be exploited in innovative devices with self-propelling and selforganizing functions, from nano to micro scales. [7][8][9][10][11][12] Myosin motors exert mechanical work based on actin filaments using the energy of ATP hydrolysis. [13] The nanometer-scale action of myosin at the same level as thermal motion is transformed to micrometer-scale sliding of actin filaments.…”

Section: Introductionmentioning

confidence: 99%

Polymer‐Carrying Ability of Actin Filaments Interacting with Myosin Motors in a Biological Motility System In Vitro

Sunada

Hatori

2022

Macromolecular Bioscience

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The reconstituted motility system of actin-myosin is expected to be used in bioinspired transport devices, in which carried materials are attached to either moving actin filaments or walking myosin molecules. However, the dependence of the ability to transport on the size of the attached materials is still inadequately understood. Here, as carried materials, polyethylene glycols (PEGs) of various sizes are covalently bound to actin filaments, and the motility of PEG-attached filaments on a heavy meromyosin (HMM) immobilized on a glass surface is observed via fluorescence microscopy. Full attachment of 2 kDa PEG, with an approximately 2 nm gyration radius, decreases the velocity and fraction of moving actin filaments by approximately 10% relative to unattached filaments. For the 5 kDa PEG, the fraction of moving filaments is decreased by approximately 70% even when the filaments contain only 20% PEG-attached actin. The attachment of both sizes of PEGs suppresses the actin-activated ATPase activity at the same level. These results suggest that actin filaments can carry PEGs up to 2 kDa having the same size as actin monomers, while the rate of ATP hydrolysis is limited. The size dependence may provide a criterion for material delivery via actin filaments in nanotransport applications.

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