Non-equilibrium assembly of microtubules: from molecules to autonomous chemical robots

Hess, Henry; Ross, Jennifer L.

doi:10.1039/c7cs00030h

Cited by 200 publications

(193 citation statements)

References 193 publications

(216 reference statements)

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“…Thus, to sustain the self‐assembled state, the cell has to supply the assemblies with energy continuously. In the case of these cytoskeletal networks, the energy comes from a chemical reaction cycle that hydrolyzes ATP or GTP (adenosine triphosphate or guanosine triphosphate) and is coupled to the self‐assembly process …”

Section: Dissipative Self‐assemblymentioning

confidence: 99%

Dissipative Self‐Assembly of Peptides

Tena‐Solsona

Boekhoven

2019

Israel Journal of Chemistry

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In molecular self‐assembly, molecules interact with each other by non‐covalent interactions to form larger structures. The process occurs in‐equilibrium, which means that molecules can leave the assembly and reassemble elsewhere, but that occurs on average with equal rates. For self‐assembly, peptides have proven to be a particularly useful building block, in part because of their versatility. Biology also uses self‐assembly to create functional materials. For example, components of the cytoskeleton, like actin filament and microtubules, are self‐assembled proteins. In other words, biology uses the same building blocks and design rules as supramolecular chemists to create functional structures. However, biological assemblies are vastly more complex than their synthetic counterparts. The discrepancy is in part because proteins are more complex than the peptides we use as building blocks. Another contributing factor to the difference in complexity is that most assemblies in living systems exist out of equilibrium. To use peptides for complex functions as biology does, we should understand and be able to create peptide assemblies out of equilibrium. In this work, we review recent advances towards the creation of peptide assemblies that exist out of equilibrium driven by an external energy source.

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Section: Dissipative Self‐assemblymentioning

confidence: 99%

Dissipative Self‐Assembly of Peptides

Tena‐Solsona

Boekhoven

2019

Israel Journal of Chemistry

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“…Microtubules are hollow tubular protein assemblies with an inner diameter of 15 nm and a length of several micrometers, which are composed of tubulin dimers (α‐ and β‐tubulin). Based on the directional movement of a motor protein kinesin along the outer surface of microtubules, artificial molecular transport systems have been established for nanodevice applications . Although the functionalization of the outer surface of microtubules has been established for nanomaterial applications, the inside of microtubules has received little attention.…”

Section: Protein‐binding Peptides Designed From Natural Proteinsmentioning

confidence: 99%

Peptide Nanomaterials Designed from Natural Supramolecular Systems

Inaba

Matsuura

2018

The Chemical Record

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Natural supramolecular assemblies exhibit unique structural and functional properties that have been optimized over the course of evolution. Inspired by these natural systems, various bio‐nanomaterials have been developed using peptides, proteins, and nucleic acids as components. Peptides are attractive building blocks because they enable the important domains of natural protein assemblies to be isolated and optimized while retaining the original structures and functions. Furthermore, the peptide subunits can be conjugated with exogenous molecules such as peptides, proteins, nucleic acids, and metal nanoparticles to generate advanced functions. In this personal account, we summarize recent progress in the construction of peptide‐based nanomaterial designed from natural supramolecular systems, including (1) artificial viral capsids, (2) self‐assembled nanofibers, and (3) protein‐binding motifs. The peptides inspired by nature should provide new design principles for bio‐nanomaterials.

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“…One way to engineer this interaction is to immobilize kinesins onto a surface to transport microtubules. With the cooperation of multiple kinesins, microtubules can glide on the surface, so‐termed gliding or motility assay (Agarwal & Hess, ; Hess & Ross, ; Jeppesen & Hoerber, ; Martin, Yu, & Van Hoozen, ; Verma, Hancock, & Catchmark, ).…”

Section: Introductionmentioning

confidence: 99%

Local direction change of surface gliding microtubules

Pan

Choi

2019

Biotech & Bioengineering

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In vitro gliding assay, microtubule translocation by kinesin motor proteins on a surface, has been used as an engineering tool in analyte detection, molecular cargo transport, and other applications. Although controlling the moving direction is often necessary to realize these applications, current direction control methods focus largely on lithographic microfabrication of tracks or external fields on the microtubules. These methods are effective, but are relatively complicated. In addition, they cannot target particular microtubules without affecting others. In this study, we propose a facile approach that can make local direction changes for selected microtubules using a polystyrene particle as a circular motion center and a DNA double helix with streptavidin as a capture arm. The DNA arm captures a microtubule in the close proximity of the immobilized particle via biotin–streptavidin interaction and changes the moving direction ~10° on average. In contrast, no significant direction changes are observed other than random variations with streptavidin‐less DNA arms (normal distribution centered at 0°), similar to regular motility assay. The particle‐assisted local direction change scheme is compared with a flow field‐based ensemble method. The combination of flow and kinesin interactions with each microtubule exerts a force to change the direction, ultimately aligning it to the flow field, regardless of its initial direction. A simple model based on the force balance predicts the time needed for such an alignment. Overall, the particle‐based local scheme is distinct and different from ensemble methods such as crossflow that changes directions of all microtubules in the field, thus offering unique utility in engineering applications.

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Non-equilibrium assembly of microtubules: from molecules to autonomous chemical robots

Cited by 200 publications

References 193 publications

Dissipative Self‐Assembly of Peptides

Dissipative Self‐Assembly of Peptides

Peptide Nanomaterials Designed from Natural Supramolecular Systems

Local direction change of surface gliding microtubules

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