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

0565321 - BFÚ 2023 RIV CH eng J - Článek v odborném periodiku
Římánková, Ludmila - Černocká, Hana - Tihlaříková, Eva - Neděla, Vilém - Ostatná, Veronika
Chronopotentiometric sensing of native, oligomeric, denatured and aggregated serum albumin at charged surfaces.
Bioelectrochemistry. Roč. 145, JUN 2022 (2022), č. článku 108100. ISSN 1567-5394. E-ISSN 1878-562X
Grant CEP: GA ČR(CZ) GA18-18154S; GA ČR(CZ) GA19-08239S
Institucionální podpora: RVO:68081707 ; RVO:68081731
Klíčová slova: Constant current chronopotentiometry * Serum albumin * Freezing * Electrode * Charged surface * Scanning transmission electron microscopy
Obor OECD: Biochemistry and molecular biology; Biochemistry and molecular biology (UPT-D)
Impakt faktor: 5, rok: 2022
Způsob publikování: Omezený přístup
https://reader.elsevier.com/reader/sd/pii/S1567539422000512?token=2776BB9FAD61EA7FFA4A4907416959A460AF8BD9CF30AEA52A04012B6503D97AEAB245621A71F06366F7B538647E27C5&originRegion=eu-west-1&originCreation=20221212135323

In 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.
Trvalý link: https://hdl.handle.net/11104/0336873