Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4661
Title: Is the monomeric prion octapeptide repeat PHGGGWGQ a specific ligand for Cu2+ ions?
Authors: Łuczkowski, M.
Kozlowski, H.
Stawikowski, M.
Rolka, K.
Gaggelli, Elena 
Valensin, Daniela 
Valensin, Gianni 
Issue Date: 2002
Project: None 
Journal: JOURNAL OF THE CHEMICAL SOCIETY. DALTON TRANSACTIONS
Abstract: 
Ac-PHGGGWGQ-NH2, an octarepeat peptide fragment of prion, is a relatively effective ligand for Cu2+ ions. At a pH of about 7.4 the major binding sites involve the imidazole nitrogen and two amide nitrogens of (3)Gly and (4)Gly giving a CuH-2L species. The stability of the complex formed is similar to other peptides having a similar type of coordination. The NMR spectra indicate that in CuH-2L the complex side chain of the Trp residue is located very close to the metal ion. The geometry around the Cu2+ ion seems to be slightly distorted from the tetragonal one. In strongly basic solution the coordination involves an additional amide nitrogen. In CuH-2L, CuH-3L and CuH-4L complexes the amide nitrogens involved in the metal ion binding are those placed towards the C-terminal from the His residue. The N-terminal of the unprotected octapeptide is very effective in binding the Cu2+ ion although at high pH the imidazole nitrogen may not be involved in metal ion binding.
Description: 
35829
URI: http://hdl.handle.net/20.500.12779/4661
ISSN: 1472-7773
DOI: 10.1039/b201040m
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.