Environmental Effects on a Prion's Helix II Domain: Copper(II) and Membrane Interactions with PrP180–193 and Its Analogues (pages 537–547)
Domenico Grasso, Giulia Grasso, Valeria Guantieri, Giuseppe Impellizzeri, Carmelo La Rosa, Danilo Milardi, Giovanni Micera, Katalin Õsz, Giuseppe Pappalardo, Enrico Rizzarelli, Daniele Sanna and Imre Sóvágó
Article first published online: 15 SEP 2005 | DOI: 10.1002/chem.200500534
The PrP180–193 (VNITIKQHTVTTTT) segment corresponding to the helix II region of the prion protein (PrP) and its shorter PrPAc184–188NH2 (IKQHT) analogue are reliable models for studying the interaction of a metal with the helix II domain (see picture). Copper(II) affinity for the PrPAc184–188NH2 fragment is higher than that of the octarepeats and PrP106–126 peptides, thus stressing the role of His187 as an anchoring binding site for this structured region of PrP.