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Royal Society of Chemistry, Dalton Transactions, 36(45), p. 14343-14351

DOI: 10.1039/c6dt02183b

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Interactions between heme and tau-derived R1 peptides: binding and oxidative reactivity

Journal article published in 2016 by V. Pirota ORCID, E. Monzani, S. Dell'Acqua, L. Casella
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

The first octadecapeptide repeat fragment of tau, R1τ, in both N-terminal amine free and acetylated forms, binds with moderate affinity to both monomeric and dimeric hemin forming 1 : 1 complexes, but does not form a 2 : 1 complex. The peroxidase activity of hemin-R1τ complexes and the effect of hemin on the aggregation properties of R1τ have been also studied.