Specificity in the Cu2+ interactions with prion protein fragments and related His-rich peptides from mammals to fishes

Copper and nickel binding in multi-histidinic peptide fragments

“…From all the spectroscopic results, the most populated states which appear at ''low" pH are in agreement with {2N The formation of macrochelates with copper binding to side chain of imidazole functions has been reported for several histidine containing peptides such as prion protein and amyloid peptides involved in neurodegenerative diseases [26,27].…”

“…As reported in the literature, the binding of three metal ions to the repeat region may be critical for the metal transport inside the cells via endocytosis mechanism [27]; by the decrease of pH as in the endosome, metal ions can be released and then reduced.…”

Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC)

“…Their complex-forming capacity has been utilized in medicine for the treatment of Wilson's disease, for the removal of excess of copper from the liver, and in the prevention of its accumulation [1][2][3][4][5][6][7]. In this paper, we present the affinities of two peptides derived from the N-terminal part of the FBP28 protein (PDB code: 1E0L) to copper (Cu 2?…”

Copper binding to chicken and human prion protein amylodogenic regions: Differences and similarities revealed by Ni2+ as a diamagnetic probe

“…Up to four Cu 2+ ions are bound within the so called ''octarepeat region" (residues 60-91) [14][15][16][17][18][19][20][21][22][23][24], and two additional ions can be bound by His residues (His-96 and His-111) outside the tandem repeat region, in the so called ''amyloidogenic" region (residues 91-126) [25][26][27][28][29][30][31][32][33]. Prion or prion-like proteins of species different from mammals showed very similar copper binding to the N-terminal tandem repeat region [34][35][36][37][38][39][40][41][42][43][44].…”