Histidine analogues of oxytocin and vasopressin as efficient ligands for Zn2+ ions – Potentiometric and NMR studies

Brasuń, Justyna; Cebrat, Marek; Jaremko, Mariusz; Jaremko, Łukasz; Gładysz, Olimpia; Zhukov, Igor

doi:10.1016/j.jinorgbio.2009.04.016

Cited by 3 publications

(1 citation statement)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The main features of the copper coordination chemistry of peptides and the roles played by His, Asp and Glu side chains have been largely discussed. 1-3,6,9-11, [13][14][15] Polyhistidine peptide fragment of zebrafish prion-like protein (PrP-rel-2) encompassing residues 74-86 with unprotected Nterminus, HTGHTGHTGSSGH-NH 2 (hereafter called zf74-86), represents an interesting ligand both for Zn 2+ and Cu 2+ ions. The N-terminal histidine residue offers the histamine-like binding site; three other histydyl residues provide the effective multi-imidazole binding site.…”

Section: Introductionmentioning

confidence: 99%

Competition between histamine-like and poly-imidazole coordination sites for Cu2+ and Zn2+ ions in zebra-fish peptide of prion-like protein

et al. 2010

View full text Add to dashboard Cite

The fragment of the zebrafish prion-like protein (PrP-rel-2), encompassing residues 74-86 and unprotected at N-terminus (zf74-86) represents a good model to understand Cu(2+) and Zn(2+) binding to ligands containing multi-potential metal donor sites. Zf(74-86) contains four His and His-1 N-terminal amine groups which constitute both copper and zinc anchoring sites. The presence of His at the first position additionally provides the histamine-like binding mode which could compete with the multi-His binding mode. In this study the speciation profiles of the Cu(2+) and Zn(2+) complexes with zf74-86 have been obtained. The main species, dominating at physiological pH, have been fully characterized by using different spectroscopic techniques. The detected NMR chemical shift variations and line broadening enhancements, caused by Zn(2+) and Cu(2+) respectively, allowed to determine the metal binding sites. Both metal ions showed common binding donor atoms, being 2 or 3 His imidazoles and the N-terminal group involved in Cu(2+) and Zn(2+) binding.

show abstract

Section: Introductionmentioning

confidence: 99%

Competition between histamine-like and poly-imidazole coordination sites for Cu2+ and Zn2+ ions in zebra-fish peptide of prion-like protein

et al. 2010

View full text Add to dashboard Cite

show abstract

The role of hydroxyl group of tyrosine in copper(II) binding by His-analogs of oxytocin

Kotynia

Czyżnikowska

Cebrat

et al. 2013

Inorganica Chimica Acta

View full text Add to dashboard Cite

Metal complexes of amino acids and peptides

Jones

Hay

Nolan³

2012

Amino Acids, Peptides and Proteins

View full text Add to dashboard Cite

This chapter deals with the most important results and observations published on various aspects of the metal complex formation with amino acids, peptides and related ligands during the past two-three years. The major sources of the references collected here are the Abstracts reported by the Web of Science Databases on the Internet but the title pages of the most common journals of inorganic, bioinorganic and coordination chemistry have also been surveyed.

show abstract

Histidine analogues of oxytocin and vasopressin as efficient ligands for Zn2+ ions – Potentiometric and NMR studies

Cited by 3 publications

References 43 publications

Competition between histamine-like and poly-imidazole coordination sites for Cu2+ and Zn2+ ions in zebra-fish peptide of prion-like protein

Competition between histamine-like and poly-imidazole coordination sites for Cu2+ and Zn2+ ions in zebra-fish peptide of prion-like protein

The role of hydroxyl group of tyrosine in copper(II) binding by His-analogs of oxytocin

Metal complexes of amino acids and peptides

Contact Info

Product

Resources

About