The structural effects of the Cys-S-S-Cys bridge exchange by the His-Cu(II)-His motif studied on natural peptides--a promising tool for natural compounds-based design

Dalton Trans. 2009 Jul 7:(25):4853-7. doi: 10.1039/b901676g. Epub 2009 May 12.

Abstract

A replacement of both Cys residues by His in oxytocin (OXT) sequence allows for the formation of the stable complex with the {NH(2), N(Im), N(Im(macrochelate))} binding mode at the physiological pH. The detailed potentiometric and spectroscopic studies on the Cu(II) complexes of [His(1,6)]OXT, together with high resolution NMR investigations on 3D structures of Cu(II) complexes with [His(1,6)]OXT and [His(1,6)]AVP analogues are presented and discussed. Exchange of the Cys-S-S-Cys bridge by the His-Cu(II)-His motif is very promising, because the resulting complexes retain topological similarity to the native S-S bridged AVP and OXT at pH values corresponding to the physiological pH.

MeSH terms

  • Amino Acid Motifs
  • Arginine / chemistry
  • Cations / chemistry
  • Circular Dichroism
  • Copper / chemistry
  • Copper / metabolism*
  • Cysteine / chemistry
  • Disulfides / chemistry
  • Electron Spin Resonance Spectroscopy
  • Histidine / chemistry*
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Oxytocin / chemistry*
  • Oxytocin / metabolism*
  • Potentiometry
  • Protein Binding
  • Protein Conformation
  • Spectrophotometry, Ultraviolet
  • Vasopressins / chemistry*
  • Vasopressins / metabolism*

Substances

  • Cations
  • Disulfides
  • Vasopressins
  • Histidine
  • Oxytocin
  • Copper
  • Arginine
  • Cysteine