Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

Santu Bera; Elad Arad; Lee Schnaider; Shira Shaham-Niv; Valeria Castelletto; Yossef Peretz; Dor Zaguri; Raz Jelinek; Ehud Gazit; Ian W. Hamley

doi:10.1039/c9cc03654g

Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

Santu Bera, Elad Arad, Lee Schnaider, Shira Shaham-Niv, Valeria Castelletto, Yossef Peretz, Dor Zaguri, Raz Jelinek, Ehud Gazit, Ian W. Hamley

Tel Aviv University, Ben-Gurion University of the Negev

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

Abstract

The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.

Original language	English
Pages (from-to)	8595-8598
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	59
DOIs	https://doi.org/10.1039/c9cc03654g
State	Published - 1 Jan 2019

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

All Science Journal Classification (ASJC) codes

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c9cc03654g

Cite this

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title = "Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core",

abstract = "The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.",

author = "Santu Bera and Elad Arad and Lee Schnaider and Shira Shaham-Niv and Valeria Castelletto and Yossef Peretz and Dor Zaguri and Raz Jelinek and Ehud Gazit and Hamley, \{Ian W.\}",

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T1 - Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

AU - Bera, Santu

AU - Arad, Elad

AU - Schnaider, Lee

AU - Shaham-Niv, Shira

AU - Castelletto, Valeria

AU - Peretz, Yossef

AU - Zaguri, Dor

AU - Jelinek, Raz

AU - Gazit, Ehud

AU - Hamley, Ian W.

PY - 2019/1/1

Y1 - 2019/1/1

N2 - The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.

AB - The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.

UR - http://www.scopus.com/inward/record.url?scp=85069479870&partnerID=8YFLogxK

U2 - 10.1039/c9cc03654g

DO - 10.1039/c9cc03654g

M3 - مقالة

SN - 1359-7345

VL - 55

SP - 8595

EP - 8598

JO - Chemical Communications

JF - Chemical Communications

IS - 59

ER -

Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

Abstract

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