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Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F19%3A10425328" target="_blank" >RIV/00216208:11320/19:10425328 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=QKq6oRe58C" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=QKq6oRe58C</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/nano9111613" target="_blank" >10.3390/nano9111613</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Fibrillar Self-Assembly of a Chimeric Elastin-Resilin Inspired Engineered Polypeptide

  • Original language description

    In the field of tissue engineering, recombinant protein-based biomaterials made up of block polypeptides with tunable properties arising from the functionalities of the individual domains are appealing candidates for the construction of medical devices. In this work, we focused our attention on the preparation and structural characterization of nanofibers from a chimeric-polypeptide-containing resilin and elastin domain, designed on purpose to enhance its cell-binding ability by introducing a specific fibronectin-derived Arg-Gly-Asp (RGD) sequence. The polypeptide ability to self-assemble was investigated. The molecular and supramolecular structure was characterized by Scanning Electronic Microscopy (SEM) and Atomic Force Microscopy (AFM), circular dichroism, state-of-the-art synchrotron radiation-induced techniques X-ray photoelectron spectroscopy (XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS). The attained complementary results allow us to assess as H-bonds influence the morphology of the aggregates obtained after the self-assembling of the chimeric polypeptide. Finally, a preliminary investigation of the potential cytotoxicity of the polypeptide was performed by culturing human fetal foreskin fibroblast (HFFF2) for its use as biomedical device.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10305 - Fluids and plasma physics (including surface physics)

Result continuities

  • Project

  • Continuities

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nanomaterials [online]

  • ISSN

    2079-4991

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    17

  • Pages from-to

    1613

  • UT code for WoS article

    000502271700108

  • EID of the result in the Scopus database

    2-s2.0-85075253624