Microchannel Systems in Titanium and Silicon for Structural and Mechanical Studies of Aligned Protein Self-Assemblies

Hirst, Linda S.; Parker, E.R.; Abu-Samah, Z.; Li, Y.; Pynn, R.; MacDonald, N.C.; Safinya, Cyrus R.

doi:10.1021/la0476175

Cited by 20 publications

(29 citation statements)

References 11 publications

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“…In addition, electric fields, shear flow, and physical confinement have also been used to align F-actin. [17][18][19][20][21] One might utilize such patterned molecular motor-cytoskeleton systems in molecular shuttle devices for the transportation of cargos which can be tethered to the molecular motor.…”

Section: 11mentioning

confidence: 99%

Self-assembled charged hydrogels control the alignment of filamentous actin

et al. 2010

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We demonstrate a novel route to control attachment of filamentous actin (F-actin) on hydrogel films. By incorporating an amine-terminated silane, the hydrogel surface charge and surface topography are varied. With increasing silane content, F-actin reorients from perpendicular to parallel to the hydrogel surface, ceases to wobble, and forms mainly elongated or cyclic structures. F-Actin coverage reaches a maximum at 2.5 vol% silane and declines at higher silane content. This biphasic behavior is explained by the simultaneous increase in surface charge and the self-assembly of a micron scale pattern of positively charged islands. Our approach provides guidelines for constructing nanoscale tracks to guide motor proteins underlying nano-engineered devices such as molecular shuttles. We demonstrate a novel route to control attachment of filamentous actin (F-actin) on hydrogel films. By incorporating an amine-terminated silane, the hydrogel surface charge and surface topography are varied. With increasing silane content, F-actin reorients from perpendicular to parallel to the hydrogel surface, ceases to wobble, and forms mainly elongated or cyclic structures. F-Actin coverage reaches a maximum at 2.5 vol% silane and declines at higher silane content. This biphasic behavior is explained by the simultaneous increase in surface charge and the self-assembly of a micron scale pattern of positively charged islands. Our approach provides guidelines for constructing nanoscale tracks to guide motor proteins underlying nano-engineered devices such as molecular shuttles.

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Section: 11mentioning

confidence: 99%

Self-assembled charged hydrogels control the alignment of filamentous actin

et al. 2010

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“…Nonetheless, cell-free experiments conducted under suitable buffer and ionic strength conditions can result in functionally significant assemblies at or near equilibrium or in kinetically trapped states, with structures similar to those occurring in vivo as determined by EM. Well-documented examples include lipids assembled into bilayer membranes exhibiting a range of shapes (40)(41)(42)(43)(44)(45), bundles of filamentous actin (7,11,(46)(47)(48)(49)(50)(51)(52)(53)(54)(55)(56) and MTs (57)(58)(59)(60)(61), and networks of NFs, all of which may show similar cell-free and in vivo structures. For example, for NF hydrogels described in this review (33)(34)(35)(36)62), variations in ionic strength, which tune the electrostatic forces in cell-free systems, qualitatively mimic the changes in intermolecular interactions in vivo, and are mediated by out-of-equilibrium enzyme-directed phosphorylation/ dephosphorylation of the NF sidearms at constant ionic strength.…”

Section: Introductionmentioning

confidence: 99%

Assembly of Biological Nanostructures: Isotropic and Liquid Crystalline Phases of Neurofilament Hydrogels

Safinya

Deek

Beck

et al. 2015

Annu. Rev. Condens. Matter Phys.

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Neurofilaments are the building blocks of the major cytoskeletal network found in the axons of vertebrate neurons. The filaments consist of three distinct molecularweight subunits-neurofilament-low, neurofilament-medium, and neurofilamenthigh-which coassemble into 10-nm flexible rods with protruding intrinsically disordered C-terminal sidearms that mediate interfilament interactions and hydrogel formation. Molecular neuroscience research includes areas focused on elucidating the functions of each subunit in network formation, during which disruptions are a hallmark of motor-neuron diseases. Here, modern concepts and methods from soft condensed matter physics are combined to address the role of subunits as it relates to interfilament forces and phase behavior in neurofilament networks. Significantly, the phase behavior studies reveal that although neurofilamentmedium subunits promote nematic liquid crystal hydrogel phase stability with parallel filament orientation, neurofilament-high subunits stabilize the hydrogel in the nematic phase close to the isotropic gel phase with random, crossed-filament orientation. This indicates a regulatory role for neurofilament-high subunits in filament orientational plasticity required for organelle (e.g., membrane-bound vesicle or mitochondrion) transport along microtubules embedded in neurofilament hydrogels. Future studies-for example, on neurofilament subunits mixed with tubulin and microtubule-associated proteins-should lead to a deeper understanding of forces and heterogeneous structures in neuronal cytoskeletons. 6.1Review in Advance first posted online on January 2, 2015. (Changes may still occur before final publication online and in print.)Changes may still occur before final publication online and in print Annu. Rev. Condens. Matter Phys. 2015.6. Downloaded from www.annualreviews.org Access provided by Selcuk University on 01/05/15. For personal use only.

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“…12 Also, self-assembly of actin bundles in confined geometries has been reported using narrow microfluidic channels. 13 In order to study hierarchical self-assembling systems like actin, which can be in different states (monomers, filaments, and networks), it is essential to have a flow-free environment in order to eliminate any possible effect on the structure formation due to induced flow fields. Some of the common procedures to eliminate possible flow are confining the actin solution in between two glass coverslips and sealing them with vacuum grease 2,14 or using hermetically sealed chambers.…”

Section: Introductionmentioning

confidence: 99%

Hierarchical self-assembly of actin in micro-confinements using microfluidics

Deshpande

Pfohl

2012

Biomicrofluidics

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We present a straightforward microfluidics system to achieve step-by-step reaction sequences in a diffusion-controlled manner in quasi two-dimensional microconfinements. We demonstrate the hierarchical self-organization of actin (actin monomers-entangled networks of filaments-networks of bundles) in a reversible fashion by tuning the Mg 2þ ion concentration in the system. We show that actin can form networks of bundles in the presence of Mg 2þ without any cross-linking proteins. The properties of these networks are influenced by the confinement geometry. In square microchambers we predominantly find rectangular networks, whereas triangular meshes are predominantly found in circular chambers. V C 2012 American Institute of Physics. [http://dx

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Microchannel Systems in Titanium and Silicon for Structural and Mechanical Studies of Aligned Protein Self-Assemblies

Cited by 20 publications

References 11 publications

Self-assembled charged hydrogels control the alignment of filamentous actin

Self-assembled charged hydrogels control the alignment of filamentous actin

Assembly of Biological Nanostructures: Isotropic and Liquid Crystalline Phases of Neurofilament Hydrogels

Hierarchical self-assembly of actin in micro-confinements using microfluidics

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