Electrochemical sensing of 2D condensation in amyloid peptides

Kurzatkowska, K., Ostatná, V., Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Doneux, T. and Palecek, E. (2013) Electrochemical sensing of 2D condensation in amyloid peptides. Electrochimica Acta, 106. pp. 43-48. ISSN 0013-4686 doi: 10.1016/j.electacta.2013.05.057

Abstract/Summary

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 −0.6 V. 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. Formation of the 2D condensed layer in peptide 1 is supported by the time, potential and temperature dependences of the interfacial capacity and it is shown that presence of the 2D layer is reflected by the peptide CPS signals due to the catalytic hydrogen evolution. The ability of peptide 1 to form the potential-dependent 2D condensed layer has been reported neither for any other peptide nor for any protein molecule. This ability might be related to the well-known oligomerization and aggregation of Alzheimer amyloid peptides.

Additional Information	Subtitle: In memory of Professor Vladimir Vetterl
Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/34122
Identification Number/DOI	10.1016/j.electacta.2013.05.057
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Additional Information	Subtitle: In memory of Professor Vladimir Vetterl
Publisher	Elsevier
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