Number of the records: 1  

Electrochemical sensing of 2D condensation in amyloid peptides

  1. 1.
    SYSNO ASEP0422785
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleElectrochemical sensing of 2D condensation in amyloid peptides
    Author(s) Kurzatkowska, K. (PL)
    Ostatná, Veronika (BFU-R) RID, ORCID
    Hamley, I.W. (GB)
    Doneux, T. (BE)
    Paleček, Emil (BFU-R) RID, ORCID
    Number of authors5
    Source TitleElectrochimica acta. - : Elsevier - ISSN 0013-4686
    Roč. 106, SEP2013 (2013), s. 43-48
    Number of pages6 s.
    Publication formPrint - P
    Languageeng - English
    CountryGB - United Kingdom
    KeywordsQUARTZ-CRYSTAL-MICROBALANCE ; SELF-ASSEMBLED MONOLAYERS ; BETA-SHEET PEPTIDES
    Subject RIVBO - Biophysics
    R&D ProjectsGAP301/11/2055 GA ČR - Czech Science Foundation (CSF)
    Institutional supportBFU-R - RVO:68081707
    UT WOS000323192400005
    DOI10.1016/j.electacta.2013.05.057
    AnnotationThe interfacial behavior of the model amyloid peptide octamer YYKLVFFC (peptide 1) and two other amyloid peptides YEVHHQKLVFF (peptide 2) and KKLVFFA (peptide 3) at the metal aqueous solution interface was studied by voltammetric and constant current chronopotentiometric stripping (CPS). All three peptides are adsorbed in a wide potential range and exhibit different interfacial organizations depending on the electrode potential. At the least negative potentials, chemisorption of peptide 1 occurs through the formation of a metal-sulfur bond. This bond is broken close to -0.6V. The peptide undergoes self-association at more negative potentials, leading to the formation of a "pit" characteristic of a 2D condensed film. Under the same conditions the other peptides do not produce such a pit.
    WorkplaceInstitute of Biophysics
    ContactJana Poláková, polakova@ibp.cz, Tel.: 541 517 244
    Year of Publishing2014
Number of the records: 1  

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