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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10.1016/j.bpc.2017.05.005

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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",

author = "F. Stellato and Z. Fusco and R. Chiaraluce and V. Consalvi and S. Dinarelli and E. Placidi and M. Petrosino and Rossi, \{G. C.\} and V. Minicozzi and S. Morante",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier B.V.",

year = "2017",

month = oct,

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

language = "English",

volume = "229",

pages = "110--114",

journal = "Biophysical Chemistry",

issn = "0301-4622",

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TY - JOUR

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

Y1 - 2017/10

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

UR - https://www.scopus.com/pages/publications/85019577254

U2 - 10.1016/j.bpc.2017.05.005

DO - 10.1016/j.bpc.2017.05.005

M3 - Article

SN - 0301-4622

VL - 229

SP - 110

EP - 114

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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