Electrochemical sensing of 2D condensation in amyloid peptides

0422785 - BFÚ 2014 RIV GB eng J - Journal Article
Kurzatkowska, K. - Ostatná, Veronika - Hamley, I.W. - Doneux, T. - Paleček, Emil
Electrochemical sensing of 2D condensation in amyloid peptides.
Electrochimica acta. Roč. 106, SEP2013 (2013), s. 43-48. ISSN 0013-4686. E-ISSN 1873-3859
R&D Projects: GA ČR(CZ) GAP301/11/2055
Institutional support: RVO:68081707
Keywords : QUARTZ-CRYSTAL-MICROBALANCE * SELF-ASSEMBLED MONOLAYERS * BETA-SHEET PEPTIDES
Subject RIV: BO - Biophysics
Impact factor: 4.086, year: 2013

The 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.
Permanent Link: http://hdl.handle.net/11104/0228926