IDEAS home Printed from https://ideas.repec.org/a/gam/jeners/v12y2019i18p3448-d264904.html
   My bibliography  Save this article

Formation of Protein Networks between Mucins: Molecular Dynamics Study Based on the Interaction Energy of the System

Author

Listed:
  • Natalia Kruszewska

    (Institute of Mathematics and Physics, UTP University of Science and Technology, Kaliskiego 7, PL-85796 Bydgoszcz, Poland)

  • Piotr Bełdowski

    (Institute of Mathematics and Physics, UTP University of Science and Technology, Kaliskiego 7, PL-85796 Bydgoszcz, Poland)

  • Piotr Weber

    (Atomic and Optical Physics Division, Department of Atomic, Molecular and Optical Physics, Faculty of Applied Physics and Mathematics, Gdańsk University of Technology, G. Narutowicza 11/12, 80-233 Gdańsk, Poland)

  • Steven Yuvan

    (Department of Physics, East Carolina University, Greenville, NC 27858, USA)

  • Marcin Drechny

    (Faculty of Telecommunications, Computer Science and Electrical Engineering, UTP University of Science and Technology, Kaliskiego 7, PL-85796 Bydgoszcz, Poland)

  • Marcin Kośmieja

    (Faculty of Telecommunications, Computer Science and Electrical Engineering, UTP University of Science and Technology, Kaliskiego 7, PL-85796 Bydgoszcz, Poland
    Nokia Solutions and Networks Sp. z o.o., Rodziny Hiszpańskich 8, PL-02685 Warszawa, Poland)

Abstract

Molecular dynamics simulations have been performed for a model aqueous solution of mucin. As mucin is a central part of lubricin, a key component of synovial fluid, we investigate its ability to form cross-linked networks. Such network formation could be of major importance for the viscoelastic properties of the soft-matter system and crucial for understanding the lubrication mechanism in articular cartilage. Thus, the inter- and intra-molecular interaction energies between the residues of mucin are analyzed. The results indicate that the mucin concentration significantly impacts its cross-linking behavior. Between 160 g/L and 214 g/L, there seems to be a critical concentration above which crowding begins to alter intermolecular interactions and their energies. This transition is further supported by the mean squared displacement of the molecules. At a high concentration, the system starts to behave subdiffusively due to network development. We also calculate a sample mean squared displacement and p -variation tests to demonstrate how the statistical nature of the dynamics is likewise altered for different concentrations.

Suggested Citation

  • Natalia Kruszewska & Piotr Bełdowski & Piotr Weber & Steven Yuvan & Marcin Drechny & Marcin Kośmieja, 2019. "Formation of Protein Networks between Mucins: Molecular Dynamics Study Based on the Interaction Energy of the System," Energies, MDPI, vol. 12(18), pages 1-18, September.
    • Handle: RePEc:gam:jeners:v:12:y:2019:i:18:p:3448-:d:264904
    as

    Download full text from publisher

    File URL: https://www.mdpi.com/1996-1073/12/18/3448/pdf
    Download Restriction: no
    File URL: https://www.mdpi.com/1996-1073/12/18/3448/
    Download Restriction: no
    ---><---

    References listed on IDEAS

    as
    1. Elio A Cino & Mikko Karttunen & Wing-Yiu Choy, 2012. "Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins," PLOS ONE, Public Library of Science, vol. 7(11), pages 1-12, November.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.

      Corrections

      All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:gam:jeners:v:12:y:2019:i:18:p:3448-:d:264904. See general information about how to correct material in RePEc.

      If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

      If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

      If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

      For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: MDPI Indexing Manager (email available below). General contact details of provider: https://www.mdpi.com .

      Please note that corrections may take a couple of weeks to filter through the various RePEc services.

      IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.