NMR Structure and CD Titration with Metal Cations of Human Prion <mml:math id="E1" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi>α</mml:mi></mml:math>2-Helix-Related Peptides

Ronga, Luisa; Palladino, Pasquale; Saviano, Gabriella; Tancredi, Teodorico; Benedetti, Ettore; Ragone, Raffaele; Rossi, Filomena

doi:https://doi.org/10.1155/2007/10720

Bioinorganic Chemistry and Applications

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Research Article | Open Access

Volume 2007 | Article ID 010720 | https://doi.org/10.1155/2007/10720

NMR Structure and CD Titration with Metal Cations of Human Prion α2-Helix-Related Peptides

Luisa Ronga,¹Pasquale Palladino,¹Gabriella Saviano,²Teodorico Tancredi,³Ettore Benedetti,¹Raffaele Ragone,⁴and Filomena Rossi¹

Academic Editor: Ivano Bertini

Received08 Mar 2007

Revised04 Jun 2007

Accepted11 Jul 2007

Published25 Sept 2007

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.

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Copyright © 2007 Luisa Ronga et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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