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Interactions of hyaladhedrins with hyaluronan and its neutral analog

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F70883521%3A28110%2F18%3A63520160" target="_blank" >RIV/70883521:28110/18:63520160 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Interactions of hyaladhedrins with hyaluronan and its neutral analog

  • Original language description

    Hyaluronic acid (HA, hyaluronan), an alternating co-polymer of glucuronic acid and N-acetylglucosamine ([4)-β-D-GlcpA-(13)-β-D-GlcpNAc-(1]n), is a major component of extracellular matrix of animal connective tissues. It plays various roles in signaling cascades and is thus involved in inflammation, progression of various diseases including cancer, and wound healing. HA-binding proteins, hyaladherins, which serve as mediators of these processes, are both membrane-bound (CD44, LYVE-1, RHAMM) or soluble (TSG-6). TSG-6 structure is known from numerous NMR experiments that indicate its interaction with HA, heparin and chondroitinsulfate [1]. We applied molecular-dynamics simulations to study the binding of HA oligosaccharides by TSG-6. Two binding sites were identified, one of which is identical with the HA-binding site described previously [2], but the other one, so far unknown, partially overlaps with the binding site of heparin [3] and also for chondroitinsulfate [1]. The specificity of the binding sites for HA and charged oligosaccharides in general was investigated by the comparison of HA with its neutral HA analog containing the glucuronic acid residue instead of glucose [4]. This molecule can be bound by both these sites, but the Helmholtz energies of complex dissociation determined by the umbrella sampling method show a remarkably lower stabilization of the analog in the first site, while in the other site the analog binding is even more stable than that of HA. The second binding site is thus less HA-specific and is able of binding various oligosaccharides independently of their negative charge. It indicates the possibility of designing artificial ligands of hyaladherins with a potential pharmaceutical application.

  • Czech name

  • Czech description

Classification

  • Type

    O - Miscellaneous

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

  • Continuities

    S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2018

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů