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.
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.
Brasuń
Justyna
J
Department of Inorganic Chemistry, Wrocław Medical University, Szewska, Poland. jbrasun@chnorg.am.wroc.pl
Cebrat
Marek
M
Jaremko
Lukasz
L
Jaremko
Mariusz
M
Ilc
Gregor
G
Gładysz
Olimpia
O
Zhukov
Igor
I
D020816:Amino Acid Motifs; D001120:Arginine / Q000737:chemistry; D002412:Cations / Q000737:chemistry; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D006639:Histidine / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010121:Oxytocin / Q000737:chemistry* / Q000378:metabolism*; D011199:Potentiometry; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D014667:Vasopressins / Q000737:chemistry* / Q000378:metabolism*
D002412:Cations; D004220:Disulfides; D014667:Vasopressins; D006639:Histidine; D010121:Oxytocin; D003300:Copper; D001120:Arginine; D003545:Cysteine