Magnetic Force-Induced Alignment of Microtubules by Encapsulation of CoPt Nanoparticles Using a Tau-Derived Peptide

Inaba, Hiroshi; Yamada, Mayuki; Rashid, Mst Rubaya; Kabir, Arif Md. Rashedul; Kakugo, Akira; Sada, Kazuki; Matsuura, Kazunori

doi:10.1021/acs.nanolett.0c01573

Cited by 24 publications

(15 citation statements)

References 52 publications

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“…The binding of TP to the interior of microtubules can be achieved by the preincubation of TP with tubulin, followed by the polymerization of the TP-tubulin complex. Thus, the conjugation of exogenous molecules, such as green fluorescent protein (GFP) ( 32 ) and magnetic cobalt-platinum nanoparticles ( 33 ), to TP can result in their encapsulation inside microtubules ( 14 ). The TP motif will be useful not only to encapsulate exogenous molecules in microtubules but also to recruit tubulins to preexisting microtubules by displaying TP on the outer surface.…”

Section: Introductionmentioning

confidence: 99%

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

et al. 2022

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Microtubules play important roles in biological functions by forming superstructures, such as doublets and branched structures, in vivo. Despite the importance, it is challenging to construct these superstructures in vitro. Here, we designed a tetrameric fluorescent protein Azami-Green (AG) fused with His-tag and Tau-derived peptide (TP), TP-AG, to generate the superstructures. Main binding sites of TP-AG can be controlled to the inside and outside of microtubules by changing the polymerization conditions. The binding of TP-AG to the inside promoted microtubule formation and generated rigid and stable microtubules. The binding of TP-AG to the outside induced various microtubule superstructures, including doublets, multiplets, branched structures, and extremely long microtubules by recruiting tubulins to microtubules. Motile microtubule aster structures were also constructed by TP-AG. The generation of various microtubule superstructures by a single type of exogenous protein is a new concept for understanding the functions of microtubules and constructing microtubule-based nanomaterials.

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Section: Introductionmentioning

confidence: 99%

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

et al. 2022

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“…Thus, the conjugation of exogenous molecules to TP can result in their encapsulation inside MTs 14 . TP has been used to encapsulate various nano-sized materials, such as green fluorescent protein (GFP) 32 , magnetic cobalt–platinum nanoparticles 33 , and gold nanoparticles 30 in MTs. The TP motif will be useful not only to encapsulate exogenous molecules in MTs, but also to recruit tubulins to pre-existing MTs by displaying TP on the outer surface.…”

Section: Introductionmentioning

confidence: 99%

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

Inaba

Sueki

Ichikawa

et al. 2022

Preprint

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Microtubules (MTs) play important roles in biological functions by forming superstructures, such as doublets, triplets, and branched structures, in vivo. Formation of these superstructures by exogenous molecules in vitro will be useful not only for understanding the functions of MTs but also as components of MT-based nanomaterials. Here, we developed a tetrameric fluorescent protein Azami-Green (AG) fused with a His-tag and Tau-derived peptide (TP), TP-AG, which can bind to the inside or outside of MTs depending on the polymerization conditions. The binding of TP-AG to the inside of MTs induced the formation, stabilized, and increased the rigidity of the MTs. The binding of TP-AG to the outside of MTs induced various types of MT superstructures, including doublets, multiplets, and branched structures, by recruiting tubulins to MTs. The formation of motile MT aster structures by TP-AG was also observed. The generation of MT superstructures by these exogenous proteins provides guidelines for the design of MT-based nanomaterials.

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“…The binding of superparamagnetic iron oxide nanoparticles provides another interesting possibility to be explored, especially because of the possibility to exert some magnetic control of the microtubule dynamics. Although, to the best of our knowledge, the application of modified ferrite nanoparticles in molecular machinery is mostly scarce to the present time (Inaba et al 2020), (Hutchins et al 2007), (Platt et al 2005, it should be mentioned that superparamagnetic nanoparticles are present in biological systems, especially in the so called magnetosomes. They are found in magnetotactic bacteria, which usually contain 15 to 20 magnetite crystals aligned in a chain enclosed by a lipid bilayer membrane.…”

Section: Introductionmentioning

confidence: 99%

Magnetic alignment of rhodamine/magnetite dual-labeled microtubules probed with inverted fluorescence microscopy

Toma

Oliveira

Melo

2022

An. Acad. Bras. Ciênc.

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Molecular machines, as exemplifi ed by the kinesin and microtubule system, are responsible for molecular transport in cells. The monitoring of the cellular machinery has attracted much attention in recent years, requiring sophisticated techniques such as optical tweezers, and dark fi eld hyperspectral and fl uorescence microscopies. It also demands suitable procedures for immobilization and labeling with functional agents such as dyes, plasmonic nanoparticles and quantum dots. In this work, microtubules were co-polymerized by incubating a tubulin mix consisting of 7 biotinylated tubulin to 3 rhodamine tubulin. Rhodamine provided the fl uorescent tag, while biotin was the anchoring group for receiving streptavidin containing species. To control the microtubule alignment and consequently, the molecular gliding directions, functionalized iron oxide nanoparticles were employed in the presence of an external magnet fi eld. Such iron oxide nanoparticles, (MagNPs) were previously coated with silica and (3-aminopro-pyl) triethoxysilane (APTS) and then modifi ed with streptavidin (SA) for linking to the biotinfunctionalized microtubules. In this way, the binding has been successfully performed, and the magnetic alignment probed by Inverted Fluorescence Microscopy. The proposed strategy has proved promising, as tested with one of the most important biological structures of the cellular machinery.

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Magnetic Force-Induced Alignment of Microtubules by Encapsulation of CoPt Nanoparticles Using a Tau-Derived Peptide

Cited by 24 publications

References 52 publications

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

Generation of stable microtubule superstructures by binding of peptide-fused tetrameric proteins to inside and outside

Magnetic alignment of rhodamine/magnetite dual-labeled microtubules probed with inverted fluorescence microscopy

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