NDLI: Copper(ii) coordination outside the tandem repeat region of an unstructured domain of chicken prion protein

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Molecular BioSystems Vol - 5 Issue - 4

Molecular BioSystems Vol - 5 Issue - 3

Molecular BioSystems Vol - 5 Issue - 2

Molecular BioSystems Vol -4

Molecular BioSystems Vol -3

Molecular BioSystems Vol -2

Copper(ii) coordination outside the tandem repeat region of an unstructured domain of chicken prion protein

Content Provider	Royal Society of Chemistry (RSC)
Author	Remelli, Maurizio Valensin, Daniela Gralka, Ewa Bacco, Dimitri Szyrwiel, Łukasz Valensin, Gianni Baranska-Rybak, Wioletta Kamasz, Wojciech Gajda, Karolina Kozłowski, Henryk
Copyright Year	2009
Abstract	Combined potentiometric, calorimetric and spectroscopic methods were used to investigate the Cu2+ binding ability and coordination behaviour of some peptide fragments related to the neurotoxic region of chicken Prion Protein. The systems studied were the following protein fragments: chPrP106–114, chPrP119–126, chPrP108–127, chPrP105–127 and chPrP105–133. The complex formation always starts around pH 4 with the coordination of an imidazole nitrogen, followed by the deprotonation and binding of amide nitrogens from the peptidic backbone. At neutral pH, the {Nim, 3N−} binding mode is the preferred one. The amide nitrogens participating in the binding to the Cu2+ ion derive from residues from the N-terminus side, with the formation of a six-membered chelate ring with the imidazolic side chain. Comparison of thermodynamic data for the two histydyl binding domains (around His-110 and His-124), clearly indicates that the closest to the hexarepeat domain (His-110) has the highest ability to bind Cu2+ ions, although both of them have the same coordination mode. Conversely, in the case of the human neurotoxic peptide region, between the two binding sites, located at His-96 and His-111, the farthest from the tandem repeat region is the strongest one. Finally, thermodynamic data show that chicken peptide is a distinctly better ligand for coordination of copper ions with respect to the human fragment.
Starting Page	497
Ending Page	510
Page Count	14
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	5
Issue Number	5
Journal	Molecular BioSystems
DOI	10.1039/b820635j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Peptide bond Ligand Tandem repeat Ion Nitrogen Protein N-terminus Neurotoxicity Nim Imidazole PH Amide Chicken Prion Copper
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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