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  1. AU="Solana, Gerardin"
  2. AU="Sill"
  3. AU="Ikler, Graham"
  4. AU="Morris Swertz"
  5. AU="Sato, Hisashi"
  6. AU="O'Rourke, Dennis H"
  7. AU="Ozuna, César"
  8. AU="Vázquez-Carrera, Manuel"
  9. AU="Tanner, Rikki M"
  10. AU="Daniel H Miller"
  11. AU="Madec, Jean-Yves"
  12. AU=Rahimi Mitra

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  1. Artikel ; Online: Biosensing using antibody-modulated motility of actin filaments on myosin-coated surfaces.

    Kekic, Murat / Hanson, Kristi L / Perumal, Ayyappasamy Sudalaiyadum / Solana, Gerardin / Rajendran, Kavya / Dash, Shantoshini / Nicolau, Dan V / Dobroiu, Serban / Dos Remedios, Cristobal G

    Biosensors & bioelectronics

    2023  Band 246, Seite(n) 115879

    Abstract: Motor proteins, such as myosin and kinesin, are biological molecular motors involved in force generation and intracellular transport within living cells. The characteristics of molecular motors, i.e., their motility over long distances, their capacity of ...

    Abstract Motor proteins, such as myosin and kinesin, are biological molecular motors involved in force generation and intracellular transport within living cells. The characteristics of molecular motors, i.e., their motility over long distances, their capacity of transporting cargoes, and their very efficient energy consumption, recommend them as potential operational elements of a new class of dynamic nano-devices, with potential applications in biosensing, analyte concentrators, and biocomputation. A possible design of a biosensor based on protein molecular motor comprises a surface with immobilized motors propelling cytoskeletal filaments, which are decorated with antibodies, presented as side-branches. Upon biomolecular recognition of these branches by secondary antibodies, the 'extensions' on the cytoskeletal filaments can achieve considerable lengths (longer than several diameters of the cytoskeletal filament carrier), thus geometrically impairing or halting motility. Because the filaments are several micrometers long, this sensing mechanism converts an event in the nanometer range, i.e., antibody-antigen sizes, into an event in the micrometer range: the visualization of the halting of motility of microns-long cytoskeletal filaments. Here we demonstrate the proof of concept of a sensing system comprising heavy-mero-myosin immobilized on surfaces propelling actin filaments decorated with actin antibodies, whose movement is halted upon the recognition with secondary anti-actin antibodies. Because antibodies to the actin-myosin system are involved in several rare diseases, the first possible application for such a device may be their prognosis and diagnosis. The results also provide insights into guidelines for designing highly sensitive and very fast biosensors powered by motor proteins.
    Mesh-Begriff(e) Actins ; Biosensing Techniques ; Actin Cytoskeleton/metabolism ; Myosins/metabolism ; Cytoskeleton/metabolism ; Antibodies/metabolism ; Kinesins/metabolism
    Chemische Substanzen Actins ; Myosins (EC 3.6.4.1) ; Antibodies ; Kinesins (EC 3.6.4.4)
    Sprache Englisch
    Erscheinungsdatum 2023-11-27
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1011023-9
    ISSN 1873-4235 ; 0956-5663
    ISSN (online) 1873-4235
    ISSN 0956-5663
    DOI 10.1016/j.bios.2023.115879
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2275: Hefte anzeigen Standort:
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  2. Artikel ; Online: Polymer surface properties control the function of heavy meromyosin in dynamic nanodevices.

    Hanson, Kristi L / Fulga, Florin / Dobroiu, Serban / Solana, Gerardin / Kaspar, Ondrej / Tokarova, Viola / Nicolau, Dan V

    Biosensors & bioelectronics

    2017  Band 93, Seite(n) 305–314

    Abstract: The actin-myosin system, responsible for muscle contraction, is also the force-generating element in dynamic nanodevices operating with surface-immobilized motor proteins. These devices require materials that are amenable to micro- and nano-fabrication, ... ...

    Abstract The actin-myosin system, responsible for muscle contraction, is also the force-generating element in dynamic nanodevices operating with surface-immobilized motor proteins. These devices require materials that are amenable to micro- and nano-fabrication, but also preserve the bioactivity of molecular motors. The complexity of the protein-surface systems is greatly amplified by those of the polymer-fluid interface; and of the structure and function of molecular motors, making the study of these interactions critical to the success of molecular motor-based nanodevices. We measured the density of the adsorbed motor protein (heavy meromyosin, HMM) using quartz crystal microbalance; and motor bioactivity with ATPase assay, on a set of model surfaces, i.e., nitrocellulose, polystyrene, poly(methyl methacrylate), and poly(butyl methacrylate), poly(tert-butyl methacrylate). A higher hydrophobicity of the adsorbing material translates in a higher total number of HMM molecules per unit area, but also in a lower uptake of water, and a lower ratio of active per total HMM molecules per unit area. We also measured the motility characteristics of actin filaments on the model surfaces, i.e., velocity, smoothness and deflection of movement, determined via in vitro motility assays. The filament velocities were found to be controlled by the relative number of active HMM per total motors, rather than their absolute surface density. The study allowed the formulation of the general engineering principles for the selection of polymeric materials for the manufacturing of dynamic nanodevices using protein molecular motors.
    Mesh-Begriff(e) Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/physiology ; Biosensing Techniques ; Myosin Subfragments/chemistry ; Myosin Subfragments/physiology ; Myosins/chemistry ; Myosins/physiology ; Nanotechnology ; Polymers/chemistry ; Quartz Crystal Microbalance Techniques ; Surface Properties
    Chemische Substanzen Myosin Subfragments ; Polymers ; Myosins (EC 3.6.4.1)
    Sprache Englisch
    Erscheinungsdatum 2017-07-15
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1011023-9
    ISSN 1873-4235 ; 0956-5663
    ISSN (online) 1873-4235
    ISSN 0956-5663
    DOI 10.1016/j.bios.2016.08.061
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 2275: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  3. Artikel: Surface hydrophobicity modulates the operation of actomyosin-based dynamic nanodevices.

    Nicolau, Dan V / Solana, Gerardin / Kekic, Murat / Fulga, Florin / Mahanivong, Chitladda / Wright, Jonathan / Ivanova, Elena P / dos Remedios, Cristobal G

    Langmuir : the ACS journal of surfaces and colloids

    2007  Band 23, Heft 21, Seite(n) 10846–10854

    Abstract: We studied the impact of surface hydrophobicity on the motility of actin filaments moving on heavy-meromyosin (HMM)-coated surfaces. Apart from nitrocellulose (NC), which is the current standard for motility assays, all materials tested are good ... ...

    Abstract We studied the impact of surface hydrophobicity on the motility of actin filaments moving on heavy-meromyosin (HMM)-coated surfaces. Apart from nitrocellulose (NC), which is the current standard for motility assays, all materials tested are good candidates for microfabrication: hydrophilic and hydrophobic glass, poly(methyl methacrylate) (PMMA), poly(tert-butyl methacrylate) (PtBuMA), and a copolymer of O-acryloyl acetophenone oxime with a 4-acryloyloxybenzophenone (AAPO). The most hydrophilic (hydrophilic glass, contact angle 35 degrees) and the most hydrophobic (PtBuMA, contact angle 78 degrees) surfaces do not maintain the motility of actin filaments, presumably because of the low density of adsorbed HMM protein or its high levels of denaturation, respectively. The velocity of actin filaments presents higher values in the middle of this "surface hydrophobicity motility window" (NC, PMMA), and a bimodal distribution, which is more apparent at the edges of this motility window (hydrophobic glass and AAPO). A molecular surface analysis of HMM and its S1 units suggests that the two very different, temporally separated conformations of the HMM heads could exacerbate the surface-modulated protein behavior, which is common to all microdevices using surface-immobilized proteins. An explanation for the above behavior proposes that the motility of actin filaments on HMM-functionalized surfaces is the result of the action of three populations of motors, each in a different surface-protein conformation, that is, HMM with both heads working (high velocities), working with one head (low velocities), and fully denatured HMM (no motility). It is also proposed that the molecularly dynamic nature of polymer surfaces amplifies the impact of surface hydrophobicity on protein behavior. The study demonstrates that PMMA is a good candidate for the fabrication of future actomyosin-driven dynamic nanodevices because it induces the smoothest motility of individual nano-objects with velocities comparable with those obtained on NC.
    Mesh-Begriff(e) Actomyosin/chemistry ; Adsorption ; Nanotechnology ; Polymers/chemistry ; Protein Denaturation ; Proteins/chemistry ; Surface Properties
    Chemische Substanzen Polymers ; Proteins ; Actomyosin (9013-26-7)
    Sprache Englisch
    Erscheinungsdatum 2007-10-09
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2005937-1
    ISSN 1520-5827 ; 0743-7463
    ISSN (online) 1520-5827
    ISSN 0743-7463
    DOI 10.1021/la700412m
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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