Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils

Yoav Raz; Boris Rubinov; Maayan Matmor; Hanna Rapaport; Gonen Ashkenasy; Yifat Miller

doi:10.1039/c3cc42879f

Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils

Yoav Raz
, Boris Rubinov
, Maayan Matmor
, Hanna Rapaport
, Gonen Ashkenasy
, Yifat Miller

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

30 Scopus citations

Abstract

The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.

Original language	English
Pages (from-to)	6561-6563
Number of pages	3
Journal	Chemical Communications
Volume	49
Issue number	58
DOIs	https://doi.org/10.1039/c3cc42879f
State	Published - 25 Jun 2013

ASJC Scopus subject areas

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/c3cc42879f

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title = "Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils",

abstract = "The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.",

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AU - Raz, Yoav

AU - Rubinov, Boris

AU - Matmor, Maayan

AU - Rapaport, Hanna

AU - Ashkenasy, Gonen

AU - Miller, Yifat

PY - 2013/6/25

Y1 - 2013/6/25

N2 - The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.

AB - The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.

UR - https://www.scopus.com/pages/publications/84879767217

U2 - 10.1039/c3cc42879f

DO - 10.1039/c3cc42879f

M3 - Article

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AN - SCOPUS:84879767217

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VL - 49

SP - 6561

EP - 6563

JO - Chemical Communications

JF - Chemical Communications

IS - 58

ER -

Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils

Abstract

ASJC Scopus subject areas

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