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Protein corona of SiO2 nanoparticles with grafted thermoresponsive copolymers: calorimetric insights on factors affecting entropy vs. enthalpy-driven associations

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F22%3A00559146" target="_blank" >RIV/61389013:_____/22:00559146 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0169433222017366?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0169433222017366?via%3Dihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.apsusc.2022.154201" target="_blank" >10.1016/j.apsusc.2022.154201</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Protein corona of SiO2 nanoparticles with grafted thermoresponsive copolymers: calorimetric insights on factors affecting entropy vs. enthalpy-driven associations

  • Original language description

    The mechanism of protein adsorption on various surfaces of tailored functionality is often accessed by isothermal titration calorimetry (ITC), the powerful tool yielding the full set of thermodynamic parameters in one label-free experiment. In this work, the non-ionic polymer brushes with thermo-switchable hydrophilic-hydrophobic balance, based on diethylene glycol methacrylate (DEGMA) and 4-vinyl pyridine (4VP) copolymers, grafted to SiO2 nanoparticles, were titrated with individual blood proteins, their mixture, and diluted human plasma. The concentration of adsorption sites was calculated from the sizes of protein molecules, assuming the formation of a monolayer. For the titrations with the protein mixture and diluted plasma, the concentration of titrant was an estimate, limiting the accuracy of thermodynamic parameters. The particles with grafted polymer brushes showed negative ξ-potentials similar to the blood proteins and their interactions occurred against the Coulomb forces. Two cases of exothermic hydrophobic and endothermic polar interactions were distinguished. The strength of adsorption, expressed with the affinity constant Ka, was dependent on brush composition and temperature. The adsorption of proteins from blood plasma was always exothermic and, therefore, the dominating hydrophobic interactions were assumed.

  • 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

    10404 - Polymer science

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Applied Surface Science

  • ISSN

    0169-4332

  • e-ISSN

    1873-5584

  • Volume of the periodical

    601

  • Issue of the periodical within the volume

    1 November

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    9

  • Pages from-to

    154201

  • UT code for WoS article

    000849603100001

  • EID of the result in the Scopus database

    2-s2.0-85134213362