Controlling the properties and self-assembly of helical nanofibrils by engineering zinc-binding β-hairpin peptides

Eyal Simonovsky; Yifat Miller

doi:10.1039/d0tb01503b

Controlling the properties and self-assembly of helical nanofibrils by engineering zinc-binding β-hairpin peptides

Eyal Simonovsky, Yifat Miller

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

6 Scopus citations

Abstract

This work illustrates a series of novel peptides that have the capability to bind Zn2+ ions and to produce fibrillar structures. The location and the type of the residues along the peptide sequence can determine the nature of the fibril. This work presents a proof-of-concept milestone for designing peptides with different properties to produce diverse materials.

Original language	English
Pages (from-to)	7352-7355
Number of pages	4
Journal	Journal of Materials Chemistry B
Volume	8
Issue number	33
DOIs	https://doi.org/10.1039/d0tb01503b
State	Published - 7 Sep 2020

ASJC Scopus subject areas

General Chemistry
Biomedical Engineering
General Materials Science

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10.1039/d0tb01503b

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title = "Controlling the properties and self-assembly of helical nanofibrils by engineering zinc-binding β-hairpin peptides",

abstract = "This work illustrates a series of novel peptides that have the capability to bind Zn2+ ions and to produce fibrillar structures. The location and the type of the residues along the peptide sequence can determine the nature of the fibril. This work presents a proof-of-concept milestone for designing peptides with different properties to produce diverse materials.",

author = "Eyal Simonovsky and Yifat Miller",

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T1 - Controlling the properties and self-assembly of helical nanofibrils by engineering zinc-binding β-hairpin peptides

AU - Simonovsky, Eyal

AU - Miller, Yifat

N1 - Publisher Copyright: © The Royal Society of Chemistry.

PY - 2020/9/7

Y1 - 2020/9/7

N2 - This work illustrates a series of novel peptides that have the capability to bind Zn2+ ions and to produce fibrillar structures. The location and the type of the residues along the peptide sequence can determine the nature of the fibril. This work presents a proof-of-concept milestone for designing peptides with different properties to produce diverse materials.

AB - This work illustrates a series of novel peptides that have the capability to bind Zn2+ ions and to produce fibrillar structures. The location and the type of the residues along the peptide sequence can determine the nature of the fibril. This work presents a proof-of-concept milestone for designing peptides with different properties to produce diverse materials.

UR - https://www.scopus.com/pages/publications/85090075840

U2 - 10.1039/d0tb01503b

DO - 10.1039/d0tb01503b

M3 - Article

C2 - 32632427

AN - SCOPUS:85090075840

SN - 2050-750X

VL - 8

SP - 7352

EP - 7355

JO - Journal of Materials Chemistry B

JF - Journal of Materials Chemistry B

IS - 33

ER -

Controlling the properties and self-assembly of helical nanofibrils by engineering zinc-binding β-hairpin peptides

Abstract

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