Issue 9, 2004
From the journal:

Dalton Transactions

The dimeric and tetrameric octarepeat fragments of prion protein behave differently to its monomeric unit†

Daniela Valensin,a   Marek Luczkowski,b   Francesca Maria Mancini,a   Anna Legowska,c   Elena Gaggelli,a   Gianni Valensin,*a   Krzysztof Rolkac  and  Henryk Kozlowski*b  

* Corresponding authors

a Department of Chemistry, University of Siena, via Aldo Moro, I-53100 Siena, Italy
E-mail: valensin@unisi.it

b Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wrocław, Poland
E-mail: henrykoz@wchuwr.chem.uni.wroc.pl

c Faculty of Chemistry, University of Gdansk, Gdansk, Poland

Abstract

Potentiometric and spectroscopic data have shown that octarepeat dimer and tetramer are much more effective ligands for Cu(II) ions than simple octapeptide. Thus, the whole N-terminal segment of prion protein due to cooperative effects, could be more effective in binding of Cu(II) than simple peptides containing a His residue. The gain of the Cu(II) binding by longer octarepeat peptides derives from the involvement of up to four imidazoles in the coordination of the first Cu(II) ion. This type of binding increases the order of the peptide structure, which allows successive metal ions for easier coordination.

Graphical abstract: The dimeric and tetrameric octarepeat fragments of prion protein behave differently to its monomeric unit

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/B402090A
Article type
Paper
Submitted
11 Feb 2004
Accepted
17 Mar 2004
First published
29 Mar 2004

Dalton Trans., 2004, 1284-1293

Permissions

Request permissions

The dimeric and tetrameric octarepeat fragments of prion protein behave differently to its monomeric unit

D. Valensin, M. Luczkowski, F. M. Mancini, A. Legowska, E. Gaggelli, G. Valensin, K. Rolka and H. Kozlowski, Dalton Trans., 2004, 1284 DOI: 10.1039/B402090A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements