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Chronopotentiometric sensing of native, oligomeric, denatured and aggregated serum albumin at charged surfaces

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    SYSNO ASEP0565321
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleChronopotentiometric sensing of native, oligomeric, denatured and aggregated serum albumin at charged surfaces
    Author(s) Římánková, Ludmila (BFU-R)
    Černocká, Hana (BFU-R) RID, ORCID
    Tihlaříková, Eva (UPT-D) RID, ORCID, SAI
    Neděla, Vilém (UPT-D) RID, ORCID, SAI
    Ostatná, Veronika (BFU-R) RID, ORCID
    Number of authors5
    Article number108100
    Source TitleBioelectrochemistry. - : Elsevier - ISSN 1567-5394
    Roč. 145, JUN 2022 (2022)
    Number of pages6 s.
    Publication formOnline - E
    Languageeng - English
    CountryCH - Switzerland
    KeywordsConstant current chronopotentiometry ; Serum albumin ; Freezing ; Electrode ; Charged surface ; Scanning transmission electron microscopy
    Subject RIVCE - Biochemistry
    OECD categoryBiochemistry and molecular biology
    Subject RIV - cooperationInstitute of Scientific Instruments - Biochemistry
    R&D ProjectsGA18-18154S GA ČR - Czech Science Foundation (CSF)
    GA19-08239S GA ČR - Czech Science Foundation (CSF)
    Method of publishingLimited access
    Institutional supportBFU-R - RVO:68081707 ; UPT-D - RVO:68081731
    UT WOS000790444700005
    EID SCOPUS85126671200
    DOI10.1016/j.bioelechem.2022.108100
    AnnotationIn protein analysis, fast techniques applicable for preliminary tests of the protein structural changes are sought. We show that using constant current chronopotentiometric stripping peak H, small amounts of oligomeric, denatured and aggregated bovine serum albumin (BSA) can be easily distinguished from native form. Different behavior of native, denatured, and aggregated BSA could be explained by combination of their different adsorption at charged surface and accessibility of electroactive amino acid residues. Ability to discriminate between individual forms allows to use chronopotentiometric stripping for study of processes responsible for structural changes, such as freezing treatment.
    WorkplaceInstitute of Biophysics
    ContactJana Poláková, polakova@ibp.cz, Tel.: 541 517 244
    Year of Publishing2023
    Electronic addresshttps://reader.elsevier.com/reader/sd/pii/S1567539422000512?token=2776BB9FAD61EA7FFA4A4907416959A460AF8BD9CF30AEA52A04012B6503D97AEAB245621A71F06366F7B538647E27C5&originRegion=eu-west-1&originCreation=20221212135323
Number of the records: 1  

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