NMR Structure and CD Titration with Metal Cations of Human Prion α2-Helix-Related Peptides. (25th September 2007)

• Record Type: Journal Article
• Authors: Ronga, Luisa; Palladino, Pasquale; Saviano, Gabriella; Tancredi, Teodorico; Benedetti, Ettore; Ragone, Raffaele; Rossi, Filomena
• Other Names: Bertini Ivano Academic Editor.
• Is Part Of: Bioinorganic chemistry and applications. Volume 2007(2007)
• Publication Date: 2007-09-25
• Subjects: Bioinorganic chemistry -- Periodicals; Bioinorganic chemistry; Biochemistry; Inorganic Chemistry; Chemistry, Bioinorganic; Periodicals; 572.51
• DOI: 10.1155/2007/10720
• Languages: English
• ISSNs: 1565-3633

Abstract

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.