The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process

F. Stellato; Z. Fusco; R. Chiaraluce; V. Consalvi; S. Dinarelli; E. Placidi; M. Petrosino; G. C. Rossi; V. Minicozzi; S. Morante

doi:10.1016/j.bpc.2017.05.005

The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process

F. Stellato, Z. Fusco, R. Chiaraluce, V. Consalvi, S. Dinarelli, E. Placidi, M. Petrosino, G. C. Rossi, V. Minicozzi^*, S. Morante

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breakers on the Aβ_1–40 peptide aggregation process in the presence of Cu^{2 +} or Zn^{2 +} transition metals. In this work we focus on two specific 5-amino acids long β-sheet breakers, namely the LPFFD Soto peptide, already known in the literature, and the LPFFN peptide recently designed and studied by our team. We provide evidence that both β-sheet breakers are effective in reducing the Aβ_1–40 aggregation propensity, even in the presence of metal ions.

Original language	English
Pages (from-to)	110-114
Number of pages	5
Journal	Biophysical Chemistry
Volume	229
DOIs	https://doi.org/10.1016/j.bpc.2017.05.005
Publication status	Published - Oct 2017

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title = "The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process",

abstract = "Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breakers on the Aβ1–40 peptide aggregation process in the presence of Cu2 + or Zn2 + transition metals. In this work we focus on two specific 5-amino acids long β-sheet breakers, namely the LPFFD Soto peptide, already known in the literature, and the LPFFN peptide recently designed and studied by our team. We provide evidence that both β-sheet breakers are effective in reducing the Aβ1–40 aggregation propensity, even in the presence of metal ions.",

keywords = "Amyloid-β peptide, Atomic Force Microscopy, Circular Dichroism, Fibrils, Inhibitors, Metal ions",

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doi = "10.1016/j.bpc.2017.05.005",

language = "English",

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T1 - The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process

AU - Stellato, F.

AU - Fusco, Z.

AU - Chiaraluce, R.

AU - Consalvi, V.

AU - Dinarelli, S.

AU - Placidi, E.

AU - Petrosino, M.

AU - Rossi, G. C.

AU - Minicozzi, V.

AU - Morante, S.

PY - 2017/10

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N2 - Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breakers on the Aβ1–40 peptide aggregation process in the presence of Cu2 + or Zn2 + transition metals. In this work we focus on two specific 5-amino acids long β-sheet breakers, namely the LPFFD Soto peptide, already known in the literature, and the LPFFN peptide recently designed and studied by our team. We provide evidence that both β-sheet breakers are effective in reducing the Aβ1–40 aggregation propensity, even in the presence of metal ions.

AB - Far-UV Circular Dichroism experiments and Atomic Force Microscopy tomography are employed to assess the impact of β-sheet breakers on the Aβ1–40 peptide aggregation process in the presence of Cu2 + or Zn2 + transition metals. In this work we focus on two specific 5-amino acids long β-sheet breakers, namely the LPFFD Soto peptide, already known in the literature, and the LPFFN peptide recently designed and studied by our team. We provide evidence that both β-sheet breakers are effective in reducing the Aβ1–40 aggregation propensity, even in the presence of metal ions.

KW - Amyloid-β peptide

KW - Atomic Force Microscopy

KW - Circular Dichroism

KW - Fibrils

KW - Inhibitors

KW - Metal ions

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DO - 10.1016/j.bpc.2017.05.005

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JO - Biophysical Chemistry

JF - Biophysical Chemistry

ER -

The effect of β-sheet breaker peptides on metal associated Amyloid-β peptide aggregation process

Abstract

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