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Characterization of the enhanced peroxidatic activity of amyloid β peptide-hemin complexes towards neurotransmitters

: Neumann, B.; Yarman, A.; Wollenberger, U.; Scheller, F.


Analytical and bioanalytical chemistry 406 (2014), Nr.14, S.3359-3364
ISSN: 1618-2642 (Print)
ISSN: 1618-2650 (Online)
Fraunhofer IBMT ()

Binding of heme to the amyloid peptides A40/42 is thought to be an initial step in the development of symptoms in the early stages of Alzheimer's disease by enhancing the intrinsic peroxidatic activity of heme. We found considerably higher acceleration of the reaction for the physiologically relevant neurotransmitters dopamine and serotonin than reported earlier for the artificial substrate 3,3,5,5-tetramethylbenzidine (TMB). Thus, the binding of hemin to A peptides might play an even more crucial role in the early stages of Alzheimer's disease than deduced from these earlier results. To mimic complex formation, a new surface architecture has been developed: The interaction between the truncated amyloid peptide A1-16 and hemin immobilized on an aminohexanethiol spacer on a gold electrode has been analyzed by cyclic voltammetry. The resulting complex has a redox pair with a 25 mV more cathodic formal potential than hemin alone.