Object's details: The N-terminus of hepcidin is a strong and potentially biologically relevant Cu(II) chelator.

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
The N-terminus of hepcidin is a strong and potentially biologically relevant Cu(II) chelator.
Creator:
Płonka, Dawid;
Bal, Wojciech
Description:
Hepcidin is an iron regulatory hormone, involved also in immune response in vertebrates. It contains the N-terminal Asp-Thr-His site able to bind Cu(II) ions. A significant discrepancy exist in the literature regarding Cu(II) affinity of this site in hepcidin. Our study focused on the model DTHFPI-NH2 hexapeptide reflecting the N-terminal motif of mature hepcidin Using potentiometry, UV-vis and CD spectroscopies we demonstrated that DTHFPI-NH2 is the strongest Cu(II) binding peptide discovered so far. A competition assay with human serum albumin (HSA) confirmed this high affinity and demonstrated that DTHFPI-NH2. withdraws all Cu(II) from HSA under equimolar concentrations. Based on these results we propose that hepcidin could exist as Cu(II) complex in blood, especially under inflammatory conditions, when its serum concentration is elevated.
Object availability:
free access
Date:
2017.06.23
Type:
Article;
PeerReviewed
Language:
English;
eng
Format:
application/msword
Publisher:
Elsevier
Relation: http://eprints.ibb.waw.pl/1429 ;http://www.sciencedirect.com/science/article/pii/S0020169317306710?via%3Dihub ;
10.1016/j.ica.2017.06.051
Subject:
QD Chemistry;
QP Physiology
Identifier: http://eprints.ibb.waw.pl/1429/1/HpcRev-final.doc ;
Płonka, Dawid and Bal, Wojciech (2017) The N-terminus of hepcidin is a strong and potentially biologically relevant Cu(II) chelator. Inorganica Chimica Acta . ISSN 0020-1693
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

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Object's details: The N-terminus of hepcidin is a strong and potentially biologically relevant Cu(II) chelator.

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