Journal
INORGANICA CHIMICA ACTA
Volume 362, Issue 3, Pages 935-945Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ica.2008.01.022
Keywords
Histidine; Sarcosine; Peptides; Macrochelate; Copper(II); Zinc(II)
Categories
Funding
- Hungarian Scientific Research Fund [OTKA T048352, T042722]
- National Office for Research and Technology [OMFB 00295/2007]
- NATO and Marie Curie Fellowships
Ask authors/readers for more resources
Copper(II) complexes of the peptides Ac-HisSarHis-NH2, Ac-HisSarHisSarHis-NH2 and Ac-HisSarHisSarHisSarHis-NH2 have been studied by potentiometric, UV-Vis, CD and EPR spectroscopic methods. Stability constants for the corresponding zinc(II) complexes have also been reported. The formation of M(II)-2N(im), M(II)-3N(im) and M(II)-4N(im) bonded macrochelates was suggested in the pH range 5-7. The macrochelates were, however, not stable enough to prevent metal ion hydrolysis in slightly alkaline solutions. In the case of copper(II) complexes, the metal ion promoted deprotonation and coordination of the amide groups of histidyl residues were also suggested. The stability constants of macrochelate complexes were compared to the literature data reported for the macrochelates of the other peptides of histidine. It was found that the thermodynamic stability of macrochelate species is largely influenced by the number and location of histidyl residues in the peptide backbone. The highest stability was obtained for the HXHYH-type sequences, while the distant arrangement of histidyl residues resulted in a significant reduction of the stability constants. (C) 2008 Elsevier B. V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available