title: NMR structure and CD titration with metal cations of human prion alpha2-helix-related peptides.
abstract: The 173-195 segment corresponding to the helix 2 of the C-globular prion protein domain could be one of several "spots" of intrinsic conformational flexibility. In fact, it possesses chameleon conformational behaviour and gathers several disease-associated point mutations. We have performed spectroscopic studies on the wild-type fragment 173-195 and on its D178N mutant dissolved in trifluoroethanol to mimic the in vivo system, both in the presence and in the absence of metal cations. NMR data showed that the structure of the D178N mutant is characterized by two short helices separated by a kink, whereas the wild-type peptide is fully helical. Both peptides retained these structural organizations, as monitored by CD, in the presence of metal cations. NMR spectra were however not in favour of the formation of definite ion-peptide complexes. This agrees with previous evidence that other regions of the prion protein are likely the natural target of metal cation binding.
authors.affiliation: Dipartimento delle Scienze Biologiche, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, Università Federico II di Napoli e Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
authors.forename: Luisa
authors.initials: L
authors.lastname: Ronga
authors.forename: Pasquale
authors.initials: P
authors.lastname: Palladino
authors.forename: Gabriella
authors.initials: G
authors.lastname: Saviano
authors.forename: Teodorico
authors.initials: T
authors.lastname: Tancredi
authors.forename: Ettore
authors.initials: E
authors.lastname: Benedetti
authors.forename: Raffaele
authors.initials: R
authors.lastname: Ragone
authors.forename: Filomena
authors.initials: F
authors.lastname: Rossi