Metal-Binding Properties of the Peptide APP170-188: A Model of the ZnII-Binding Site of Amyloid Precursor Protein (APP)

2005 ◽  
Vol 11 (3) ◽  
pp. 903-909 ◽  
Author(s):  
Eliza-Diana Ciuculescu ◽  
Yasmina Mekmouche ◽  
Peter Faller
Metallomics ◽  
2018 ◽  
Vol 10 (1) ◽  
pp. 108-119 ◽  
Author(s):  
Tessa R. Young ◽  
Anthony G. Wedd ◽  
Zhiguang Xiao

APP E2 forms stable Cu(i)-mediated ternary complexes with several competing ligands, but not upon addition of heparin. This allows a systematic review of general conditions for quantification of metal–protein affinity and new insights into the physiological functions of APP.


2004 ◽  
pp. 16-22 ◽  
Author(s):  
Daniela Valensin ◽  
Francesca Maria Mancini ◽  
Marek Łuczkowski ◽  
Anna Janicka ◽  
Kornelia Wiśniewska ◽  
...  

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5221
Author(s):  
Salvatore La Gatta ◽  
Linda Leone ◽  
Ornella Maglio ◽  
Maria De Fenza ◽  
Flavia Nastri ◽  
...  

Understanding the structural determinants for metal ion coordination in metalloproteins is a fundamental issue for designing metal binding sites with predetermined geometry and activity. In order to achieve this, we report in this paper the design, synthesis and metal binding properties of METP3, a homodimer made up of a small peptide, which self assembles in the presence of tetrahedrally coordinating metal ions. METP3 was obtained through a redesign approach, starting from the previously developed METP molecule. The undecapeptide sequence of METP, which dimerizes to house a Cys4 tetrahedral binding site, was redesigned in order to accommodate a Cys2His2 site. The binding properties of METP3 were determined toward different metal ions. Successful assembly of METP3 with Co(II), Zn(II) and Cd(II), in the expected 2:1 stoichiometry and tetrahedral geometry was proven by UV-visible spectroscopy. CD measurements on both the free and metal-bound forms revealed that the metal coordination drives the peptide chain to fold into a turned conformation. Finally, NMR data of the Zn(II)-METP3 complex, together with a retrostructural analysis of the Cys-X-X-His motif in metalloproteins, allowed us to define the model structure. All the results establish the suitability of the short METP sequence for accommodating tetrahedral metal binding sites, regardless of the first coordination ligands.


1995 ◽  
Vol 270 (45) ◽  
pp. 26774-26777 ◽  
Author(s):  
Mariagrazia Grilli ◽  
Marina Ribola ◽  
Antonella Alberici ◽  
Alessandra Valerio ◽  
Maurizio Memo ◽  
...  

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Magdalena Sokołowska ◽  
Krystyna Pawlas ◽  
Wojciech Bal

Visible-range circular dichroism titrations were used to study Cu(II) binding properties of Multimetal Binding Site (MBS) of Human Serum Albumin (HSA). The formation of ternary MBS-Cu(II)-Buffer complexes at pH 7.4 was positively verified for sodium phosphate, Tris, and Hepes, the three most common biochemical buffers. The phosphate > Hepes > Tris order of affinities, together with strong spectral changes induced specifically by Tris, indicates the presence of both Buffer-Cu(II) and Buffer-HSA interactions. All complexes are strong enough to yield a nearly 100% ternary complex formation in 0.5 mM HSA dissolved in 100 mM solutions of respective buffers. The effects of warfarin and ibuprofen, specific ligands of hydrophobic pockets I and II in HSA on the Cu(II) binding to MBS were also investigated. The effects of ibuprofen were negligible, but warfarin diminished the MBS affinity for Cu(II) by a factor of 20, as a result of indirect conformational effects. These results indicate that metal binding properties of MBS can be modulated directly and indirectly by small molecules.


2013 ◽  
Vol 78 (11) ◽  
pp. 1263-1271 ◽  
Author(s):  
O. V. Bocharova ◽  
A. S. Urban ◽  
K. D. Nadezhdin ◽  
E. V. Bocharov ◽  
A. S. Arseniev

2012 ◽  
Vol 416 (3) ◽  
pp. 438-452 ◽  
Author(s):  
Sven O. Dahms ◽  
Ina Könnig ◽  
Dirk Roeser ◽  
Karl-Heinz Gührs ◽  
Magnus C. Mayer ◽  
...  

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