Multi-histidinic fragments binding biological metals: an NMR study

TL;DRAbstract

Cap43 protein can be considered as a “stress protein” since it is involved in a number of noxious events inside the cell, like hypoxia, cancerous states and metastasis
\nsuppression, and stress response just to quote some. Another interesting feature is that its expression is triggered by the rise in concentration of some metals, amongst which nickel gives the highest response.
\n<br>We have examined the whole sequence of this protein in the search of a suitable site for metal binding, finding a remarkable aspect that prompted us to deepen our
\ninvestigation. In fact, Cap43 presents in its C-terminal region a mono-histidinic decapeptide whose sequence is repeated consecutively three times (TRSRSHTSEGTRSRSHTSEG-
\nTRSRSHTSEG). The occurrence of such a repeated motif containing a histidine residue reminded us of neurodegenerative deseases and prions, where an
\noctapeptide fragment bearing an histidine residue is repeated four times, and proved to be very a

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