Literature DB >> 21980910

pH-Dependent Cu(II) coordination to amyloid-β peptide: impact of sequence alterations, including the H6R and D7N familial mutations.

Bruno Alies1, Hélène Eury, Christian Bijani, Lionel Rechignat, Peter Faller, Christelle Hureau.   

Abstract

Copper ions have been proposed to intervene in deleterious processes linked to the development of Alzheimer's disease (AD). As a direct consequence, delineating how Cu(II) can be bound to amyloid-β (Aβ) peptide, the amyloidogenic peptide encountered in AD, is of paramount importance. Two different forms of [Cu(II)(Aβ)] complexes are present near physiological pH, usually noted components I and II, the nature of which is still widely debated in the literature, especially for II. In the present report, the phenomenological pH-dependent study of Cu(II) coordination to Aβ and to ten mutants by EPR, CD, and NMR techniques is described. Although only indirect insights can be obtained from the study of Cu(II) binding to mutated peptides, they reveal very useful for better defining Cu(II) coordination sites in the native Aβ peptide. Four components were identified between pH 6 and 12, namely, components I, II, III and IV, in which the predominant Cu(II) equatorial sites are {-NH(2), CO (Asp1-Ala2), N(im) (His6), N(im) (His13 or His14)}, {-NH(2), N(-) (Asp1-Ala2), CO (Ala2-Glu3), N(im)}, {-NH(2), N(-) (Asp1-Ala2), N(-) (Ala2-Glu3), N(im)} and {-NH(2), N(-) (Asp1-Ala2), N(-) (Ala2-Glu3), N(-) (Glu3-Phe4)}, respectively, in line with classical pH-induced deprotonation of the peptide backbone encountered in Cu(II) peptidic complexes formation. The structure proposed for component II is discussed with respect to another coordination model reported in the literature, that is, {CO (Ala2-Glu3), 3 N(im)}. Cu(II) binding to the H6R-Aβ and D7N-Aβ peptides, where the familial H6R and D7N mutations have been linked to early onset of AD, has also been investigated. In case of the H6R mutation, some different structural features (compared to those encountered in the native [Cu(II)(Aβ)] species) have been evidenced and are anticipated to be important for the aggregating properties of the H6R-Aβ peptide in presence of Cu(II).
© 2011 American Chemical Society

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Year:  2011        PMID: 21980910     DOI: 10.1021/ic201739n

Source DB:  PubMed          Journal:  Inorg Chem        ISSN: 0020-1669            Impact factor:   5.165


  15 in total

1.  Calorimetric investigation of copper(II) binding to Aβ peptides: thermodynamics of coordination plasticity.

Authors:  Cristina Sacco; Rachel A Skowronsky; Sunitha Gade; John M Kenney; Anne M Spuches
Journal:  J Biol Inorg Chem       Date:  2012-01-22       Impact factor: 3.358

2.  The effect of Cu(2+) and Zn(2+) on the Aβ42 peptide aggregation and cellular toxicity.

Authors:  Anuj K Sharma; Stephanie T Pavlova; Jaekwang Kim; Jungsu Kim; Liviu M Mirica
Journal:  Metallomics       Date:  2013-11       Impact factor: 4.526

3.  Copper(II)-bis-histidine coordination structure in a fibrillar amyloid β-peptide fragment and model complexes revealed by electron spin echo envelope modulation spectroscopy.

Authors:  Jessica Hernández-Guzmán; Li Sun; Anil K Mehta; Jijun Dong; David G Lynn; Kurt Warncke
Journal:  Chembiochem       Date:  2013-09-06       Impact factor: 3.164

Review 4.  APP/Aβ structural diversity and Alzheimer's disease pathogenesis.

Authors:  Alex E Roher; Tyler A Kokjohn; Steven G Clarke; Michael R Sierks; Chera L Maarouf; Geidy E Serrano; Marwan S Sabbagh; Thomas G Beach
Journal:  Neurochem Int       Date:  2017-08-12       Impact factor: 3.921

5.  Local structure and global patterning of Cu2+ binding in fibrillar amyloid-β [Aβ(1-40)] protein.

Authors:  William A Gunderson; Jessica Hernández-Guzmán; Jesse W Karr; Li Sun; Veronika A Szalai; Kurt Warncke
Journal:  J Am Chem Soc       Date:  2012-10-24       Impact factor: 15.419

6.  Copper ligation to soluble oligomers of the English mutant of the amyloid-β peptide yields a linear Cu(I) site that is resistant to O2 oxidation.

Authors:  Kristy L Peck; Heather S Clewett; Jennifer C Schmitt; Jason Shearer
Journal:  Chem Commun (Camb)       Date:  2013-05-25       Impact factor: 6.222

7.  Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.

Authors:  Elena Atrián-Blasco; Paulina Gonzalez; Alice Santoro; Bruno Alies; Peter Faller; Christelle Hureau
Journal:  Coord Chem Rev       Date:  2018-09-15       Impact factor: 22.315

8.  Link between Affinity and Cu(II) Binding Sites to Amyloid-β Peptides Evaluated by a New Water-Soluble UV-Visible Ratiometric Dye with a Moderate Cu(II) Affinity.

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Journal:  Anal Chem       Date:  2017-01-25       Impact factor: 6.986

Review 9.  Multi-Target Directed Donepezil-Like Ligands for Alzheimer's Disease.

Authors:  Mercedes Unzeta; Gerard Esteban; Irene Bolea; Wieslawa A Fogel; Rona R Ramsay; Moussa B H Youdim; Keith F Tipton; José Marco-Contelles
Journal:  Front Neurosci       Date:  2016-05-25       Impact factor: 4.677

10.  Modulation of amyloid-β aggregation by metal complexes with a dual binding mode and their delivery across the blood-brain barrier using focused ultrasound.

Authors:  Tiffany G Chan; Carmen L Ruehl; Sophie V Morse; Michelle Simon; Viktoria Rakers; Helena Watts; Francesco A Aprile; James J Choi; Ramon Vilar
Journal:  Chem Sci       Date:  2021-06-15       Impact factor: 9.825

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