These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: The unusual binding abilities of the His-analogue of Arg-vasopressin towards Cu2+.
    Author: Brasuń J, Cebrat M, Sochacka A, Gładysz O, Swiatek-Kozłowska J.
    Journal: Dalton Trans; 2008 Oct 07; (37):4978-80. PubMed ID: 18802608.
    Abstract:
    A new vasopressin analogue, [His1,6]AVP, was synthesized and characterized by potentiometric measurements as well as by UV-Vis, CD and EPR spectroscopy. At the physiological pH the peptide forms a stable complex with Cu2+ ions which is characterized by the {NH2, NIm, NIm(macrochelate)} binding mode. The replacement of both Cys by His residues in the vasopressin sequence results in a very significant increase in the efficiency of Cu2+ binding.
    [Abstract] [Full Text] [Related] [New Search]