Actomyosin motility on nanostructured surfaces

Bunk, Richard; Klinth, Jeanna; Montelius, Lars; Nicholls, Ian A.; Omling, P.; Tågerud, Sven; Månsson, Alf

doi:10.1016/s0006-291x(03)00027-5

Cited by 75 publications

(130 citation statements)

References 24 publications

Supporting

Mentioning

123

Contrasting

Order By: Relevance

“…The motility of actin filaments powered by myosin or its fragments, such as heavy meromyosin (HMM), has been demonstrated on various surfaces, which include nitrocellulose, [72,76] glass, [33,64] poly(methyl methacrylate) (PMMA), [32] poly(tertbutyl methacrylate) (PtBuMA), poly(methacrylic acid) (PMAA), [34] poly(tetrafluoroethylene) (PTFE), [31] O-acryloyl acetophenone oxime (AAPO) copolymer, [82,83] printable crosslinkable UV-resist (MRL-6000), [84] and glass surfaces derivatized with trimethylchlorosilane (TMCS). [85,86] Similarly, the motility of microtubules powered by kinesin has also been demonstrated on surfaces, such as glass, [75,[87][88][89][90][91] PTFE, [35] deepUV resist (SAL601), [37] silicon, [87] PMMA, [88] poly(dimethylsiloxane) (PDMS), [88] ethylene-vinyl alcohol copolymer (EVOH), [88] thermoresponsive poly(Nisopropylacrylamide) (PNIPAM) grafted onto polyglycidyl methacrylate (PGMA), [92] and reconstituted microtubules.…”

Section: Surface Effectsmentioning

confidence: 99%

“…[93] Some features worth noting are that different surfaces induce differential adsorption of proteins (i.e., BSA and motors) and small variations in experimental conditions can lead to entirely different motilities. For instance, several authors [32,34] demonstrated the motility of actin filaments on patterned PMMA, whereas others [84] used PMMA for patterns that do not support motility. The difference in experimental results, which is less evident for hard surfaces, such as glass and silicon, derives from the complex character of polymers and their surfaces.…”

Section: Surface Effectsmentioning

confidence: 99%

“…[111] The second technological choice was implemented in an early study [32] by preferential adsorption of HMM on PMMAmicrofabricated features on a non-adhesive glass background. Most studies, however, couple the patterning of motor proteins with the mechanical confinement of motility in profiled microfabricated micro-channels, which has been achieved for HMM/myosin for several architectures, e.g., (i) floor: hydrophobic glass, walls: PMMA; [33] (ii) floor: hydrophobic glass, walls: BSA-coated ablated AAPO copolymer; [82,83] (iii) floor: UVresist (MRL-6000), walls: PMMA; [84] (iv) floor: glass, walls: metal electrodes; [113] and more recently (v) floor: TMCSSiO 2 , walls: lift-off resist (LOR070A) and PMMA. [112,114] Similarly, kinesin immobilization in micro-channels has been demonstrated for (i) floor: SiO 2 , walls: PEO-coated SU8 (photoresist); [111] (ii) floor: glass, walls: SAL601 (e-beam resist); [37] and (iii) floor: glass, walls: SU8.…”

Section: Lateral Confinement Of Movement Formentioning

confidence: 99%

See 2 more Smart Citations

Protein Linear Molecular Motor‐Powered Nanodevices

Bakewell

Nicolau

2007

ChemInform

View full text Add to dashboard Cite

Myosin-actin and kinesin-microtubule linear protein motor systems and their application in hybrid nanodevices are reviewed. Research during the past several decades has provided a wealth of understanding about the fundamentals of protein motors that continues to be pursued. It has also laid the foundations for a new branch of investigation that considers the application of these motors as key functional elements in laboratory-on-a-chip and other micro/nanodevices. Current models of myosin and kinesin motors are introduced and the effects of motility assay parameters, including temperature, toxicity, and in particular, surface effects on motor protein operation, are discussed. These parameters set the boundaries for gliding and bead motility assays. The review describes recent developments in assay motility confinement and unidirectional control, using micro-and nano-fabricated structures, surface patterning, microfluidic flow, electromagnetic fields, and self-assembled actin filament/microtubule tracks. Current protein motor assays are primitive devices, and the developments in governing control can lead to promising applications such as sensing, nano-mechanical drivers, and biocomputation.

show abstract

Section: Surface Effectsmentioning

confidence: 99%

Section: Surface Effectsmentioning

confidence: 99%

Section: Lateral Confinement Of Movement Formentioning

confidence: 99%

See 1 more Smart Citation

Protein Linear Molecular Motor‐Powered Nanodevices

Bakewell

Nicolau

2007

ChemInform

View full text Add to dashboard Cite

show abstract

“…The sidewall collisions described above and the subsequent guidance of microtubules along the sidewall were well characterized by [49]. Similar nano-structured surfaces were also used for the actomyosin system [40] although actin filaments often climbed up the wall and escaped from tracks owing to their lower flexural rigidity compared with microtubules. This limitation has been overcome by shaping the surface morphology with nanometer precision, which forces the filaments to move exclusively on the tracks [51].…”

Section: Controlling the Direction Of Protein Filament Movement Usingmentioning

confidence: 99%

“…In order to control the track along which filaments glide, it is necessary to restrict the location of active motors to specific regions of the surface. While the detailed interactions of motor proteins with surfaces are not well understood, it has been observed that myosin motility is primarily restricted to the more hydrophobic resist surfaces [40,41]. Thus, myosin and proteolytic fragments of myosin can be readily aligned on polytetrafluoroethylene (PTFE)-deposited surfaces, resulting in the movement of actin filaments being restricted to the well-defined fabricated tracks [42].…”

Section: Controlling the Direction Of Protein Filament Movement Usingmentioning

confidence: 99%

How Linear Motor Proteins Work

Oiwa

Manstein

Controlled Nanoscale Motion

View full text Add to dashboard Cite

Most animals perform sophisticated forms of movement such as walking, running, flying and swimming using their skeletal muscles. Although directed movement is not generally associated with plants, cytoplasmic streaming in plant cells can reach velocities greater than 50 µm/s and thus constitutes one of the fastest forms of directed movement. Unicellular eukaryotic organisms and prokaryotes display diverse mechanisms by which they are able to actively move towards a food source, light or other sensory stimuli. On the cellular level active transport of vesicles and organelles is required, since the cytoplasm resembles a gel with a mesh size of approximately 50 nm, which makes the passive transport of organelle-sized particles impossible. For elongated cells such as neurons, even proteins and small metabolites have to be actively transported.Linear motor proteins, moving on cytoskeletal filaments such as actin filaments and microtubules, are predominantly responsible for the motile activity in eukaryotic cells. They are chemo-mechanical enzymes that use the chemical energy from adenosinetriphosphate (ATP) hydrolysis to generate force and to move cargoes along their filament tracks. Under physiological conditions, the energy input per molecule of ATP corresponds to the chemical free energy liberated by its hydrolysis to adenosinediphosphate (ADP) and inorganic phosphate (P i ), ca. 10 −19 J (100 pNnm). The thermodynamic efficiency of motor proteins varies between 30 and 60%. As machines, motor proteins are unique since they convert chemical energy to mechanical work directly, rather than through an intermediate such as heat or electrical energy. Structural Features of Cytoskeletal Motor ProteinsThree families of linear, cytoskeletal motor proteins have been described: kinesin, dynein, and myosin ( Fig. 3.1). Kinesin and dynein family members K. Oiwa and D

show abstract