Zoroddu, Maria Antonietta and Peana, Massimiliano Francesco and Medici, Serenella and Solinas, Costantino and Juliano, Claudia Clelia Assunta and Anedda, Roberto and Nurchi, Valeria Marina and Crisponi, Guido (2012) Coordination abilities of mono and multi-histidinic and glutamate peptide fragments towards manganese(II) and cobalt(II). In: ISMEC 2012: 23. International symposium on metal complexes, 18-22 June 2012, Lisbon, Portugal. [S.l.], ISMEC Group / Universidade Técnica de Lisboa. p. 200-201. (ISMEC Group Series, 2). ISSN 2239-2459. Conference or Workshop Item.
It is known that rich repeat domains in peptides can be of interest as the models for the study of molecular phenomena related to metal ion binding in proteins involved in
neurodegenerative disorders. Imbalances in transition metal ions are assumed to contribute to the conversion of the multi-histidinic amyloid β-peptide (Aβ) from its soluble form to an amyloidogenic form, and to Aβ deposition. Of these ions, it has been reported that manganese binding to PrP is detrimental and causes a conformational change in the protein, suggesting that manganese binding could potentially play a role in prion disease progression in vivo. It appears that PrP is less stable on binding manganese and quickly converts to a misfolded form. The binding of manganese to PrP potentially results in the conversion of the protein to an abnormal isoform with properties reminiscent of PrPsc. In particular, although PrP can bind the same number of manganese atoms as of copper atoms, the resulting protein becomes proteinase resistant, forms fibrils and loses function.[1,2]
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