JBIC Journal of Biological Inorganic Chemistry

, Volume 16, Issue 2, pp 333–340 | Cite as

Zinc(II) modulates specifically amyloid formation and structure in model peptides

  • Bruno Alies
  • Vincent Pradines
  • Isabelle Llorens-Alliot
  • Stéphanie Sayen
  • Emmanuel Guillon
  • Christelle HureauEmail author
  • Peter FallerEmail author
Original Paper


Metal ions such as zinc and copper can have dramatic effects on the aggregation kinetics of and the structures formed by several amyloidogenic peptides/proteins. Depending on the identity of the amyloidogenic peptide/protein and the conditions, Zn(II) and Cu(II) can promote or inhibit fibril formation, and in some cases these metal ions have opposite effects. To better understand this modulation of peptide aggregation by metal ions, the impact of Zn(II) binding to three amyloidogenic peptides (Aβ14-23, Aβ11-23, and Aβ11-28) on the formation and structure of amyloid-type fibrils was investigated. Zn(II) was able to accelerate fibril formation for all three peptides as measured by thioflavin T fluorescence and transmission electron microscopy. The effects of Zn(II) on Aβ11-23 and Aβ11-28 aggregation were very different compared with the effects of Cu(II), showing that these promoting effects were metal-specific. X-ray absorption spectroscopy suggested that the Zn(II) binding to Aβ11-23 and Aβ11-28 is very different from Cu(II) binding, but that the binding is similar in the case of Aβ14-23. A model is proposed in which the different coordination chemistry of Zn(II) compared with Cu(II) explains the metal-specific effect on aggregation and the difference between peptides Aβ14-23 and Aβ11-23/Aβ11-28.


Amyloid Zinc Copper Aggregation Spectroscopy 


Amyloid β


European Synchrotron Radiation Facility


Extended X-ray absorption fine structure


4-(2-Hydroxyethyl)-1-piperazineethanesulfonic acid


Piperazine-1,4-bis-(2-hydroxy-propane-sulfonic acid) dihydrate


Thioflavin T


X-ray absorption spectroscopy



We acknowledge the ESRF for beamtime provision and the team of beamline FAME 30B, especially Olivier Proux, for their helpful support. We also thank Thomas Lunardi and the EMBL laboratory (Grenoble) for their support in performing UV–vis spectroscopy near the beamline, and Vincent Colliere and Diana Ciuculescu (LCC Toulouse) for part of the transmission electron microscopy experiments. This work was supported by the ESRF (Experiment CH-3015), a grant from the French Ministry (MERT) (B.A.), and a grant from the Agence Nationale de la Recherche (ANR) Programme Blanc NT09-488591, “NEUROMETALS” (P.F. and C.H.).

Supplementary material

775_2010_729_MOESM1_ESM.pdf (219 kb)
Supplementary material 1 (PDF 219 kb)


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Copyright information

© SBIC 2010

Authors and Affiliations

  • Bruno Alies
    • 1
    • 2
  • Vincent Pradines
    • 1
    • 2
  • Isabelle Llorens-Alliot
    • 3
  • Stéphanie Sayen
    • 4
  • Emmanuel Guillon
    • 4
  • Christelle Hureau
    • 1
    • 2
    Email author
  • Peter Faller
    • 1
    • 2
    Email author
  1. 1.LCC (Laboratoire de Chimie de Coordination), CNRSToulouseFrance
  2. 2.Université de Toulouse, UPS, INPTToulouseFrance
  3. 3.CEA/DSM/INAC/NRSGrenobleFrance
  4. 4.Institut de Chimie Moléculaire de Reims (ICMR, CNRS UMR 6229), Groupe Chimie de CoordinationUniversité de Reims Champagne-ArdenneReims Cedex 2France

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