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Revisiting Cu(II) Bound Amyloid-β40 and Amyloid-β42 Peptides: Varying Coordination Chemistries

Yıl 2018, Cilt: 5 Sayı: 3, 981 - 1008, 01.09.2018
https://doi.org/10.18596/jotcsa.424144

Öz





Metal ions and intrinsically disordered peptides amyloid-β40
and amyloid-β42 are at the center of Alzheimer´s disease pathology. Divalent
copper ion binds to amyloid-β40 and amyloid-β42 peptides with varying
coordination chemistries. Experiments face challenges in the measurements of
divalent copper ion bound monomeric amyloid-β40 and amyloid-β42 in an aqueous
solution medium because of fast conformational changes, rapid aggregation
processes and solvent effects. Theoretical studies complement experiments and
provide insights at the atomic and molecular levels with dynamics. However,
until recently, potential functions for simulating divalent copper ion bound
amyloid-β40 and amyloid-β42 peptides with varying coordination chemistries were
lacking. Using new potential functions that were developed for divalent copper
centers, Cu(II), including three histidine residues and an oxygen-ligated amino
acid residue, the structures and thermodynamic properties of Cu(II)-bound
amyloid-β40 and amyloid-β42 peptides in an aqueous solution medium were
studied. For these purposes, extensive first principles calculations and
replica exchange molecular dynamics simulations were conducted. In this study,
the secondary and tertiary structural properties, conformational Gibbs free
energy values, potential of mean force surfaces, salt bridges and aggregation
propensities of aqueous Cu(II)-bound amyloid-β40 and amyloid-β42 peptides are
presented. Different than previous findings in the literature, results clearly
show that the coordination chemistry variations impact the structural and
thermodynamic properties of divalent Cu(II) bound amyloid-β alloforms in water.
Specificities about these differences are revealed in this study at the atomic
level with dynamics. Results presented herein are the first to offer a
comparison of the monomeric Cu(II)-bound amyloid-β40 and amyloid-β42 peptides
with varying coordination chemistries using bonded model potential functions.




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Yıl 2018, Cilt: 5 Sayı: 3, 981 - 1008, 01.09.2018
https://doi.org/10.18596/jotcsa.424144

Öz

Kaynakça

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  • 115. Nagypal I, Gergely A, Farkas E. Thermodynamic Study of Parent and Mixed Complexes of Aspartic-acid, Glutamic-acid and Glycine with Copper(II). Journal of Inorganic & Nuclear Chemistry. 1974 ;36:699-706.
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  • 132. Boopathi S, Kolandaivel P. Role of zinc and copper metal ions in amyloid β-peptides Aβ1–40 and Aβ1–42 aggregation. RSC Adv. 2014 Aug;4:38951-38965.
  • 133. Dong M, Li H, Hu D, Zhao W, Zhu W, Ai H. Molecular Dynamics Study on the Inhibition Mechanisms of Drugs CQ1–3 for Alzheimer Amyloid-β40 Aggregation Induced by Cu2+. ACS Chem. Neurosci. 2016 Feb;7:599-614.
  • 134. Velez-Vega C, Escobedo F. A. Characterizing the Structural Behavior of Selected Aβ-42 Monomers with Different Solubilities. J. Phys. Chem. B. 2011 Apr;115:4900-4910.
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  • 136. Sgourakis N. G, Yan Y, McCallum S. A, Wang C, Garcia A. E. The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR study. J. Mol. Biol. 2007 May;368:1448-1457. 137. Yan Y, Wang C. Abeta42 is more rigid than Abeta40 at the C terminus: implications for Abeta aggregation and toxicity. J. Mol. Biol. 2006 Dec;364:853-862.
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  • 139. Mantri Y, Fioroni M, Baik M-H. Computational study of the binding of CuII to Alzheimer's amyloid-beta peptide: do Abeta42 and Abeta40 bind copper in identical fashion? J. Biol. Inorg. Chem. 2008 Nov;13:1197-1204.
Toplam 138 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Konular Kimya Mühendisliği
Bölüm Makaleler
Yazarlar

Orkid Coskuner-weber 0000-0002-0772-9350

Yayımlanma Tarihi 1 Eylül 2018
Gönderilme Tarihi 16 Mayıs 2018
Kabul Tarihi 16 Ağustos 2018
Yayımlandığı Sayı Yıl 2018 Cilt: 5 Sayı: 3

Kaynak Göster

Vancouver Coskuner-weber O. Revisiting Cu(II) Bound Amyloid-β40 and Amyloid-β42 Peptides: Varying Coordination Chemistries. JOTCSA. 2018;5(3):981-1008.