Self-assembly and Self-replication of Short Amphiphilic β-sheet Peptides

Valery Bourbo; Maayan Matmor; Elina Shtelman; Boris Rubinov; Nurit Ashkenasy; Gonen Ashkenasy

doi:10.1007/s11084-011-9257-y

Self-assembly and Self-replication of Short Amphiphilic β-sheet Peptides

Valery Bourbo, Maayan Matmor, Elina Shtelman, Boris Rubinov, Nurit Ashkenasy, Gonen Ashkenasy

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

19 Scopus citations

Abstract

Most self-replicating peptide systems are made of α-helix forming sequences. However, it has been postulated that shorter and simpler peptides may also serve as templates for replication when arranged into well-defined structures. We describe here the design and characterization of new peptides that form soluble β-sheet aggregates that serve to significantly accelerate their ligation and self-replication. We then discuss the relevance of these phenomena to early molecular evolution, in light of additional functionality associated with β-sheet assemblies.

Original language	English
Pages (from-to)	563-567
Number of pages	5
Journal	Origins of Life and Evolution of Biospheres
Volume	41
Issue number	6
DOIs	https://doi.org/10.1007/s11084-011-9257-y
State	Published - 1 Dec 2011

Keywords

Prebiotic peptides
Self-replication
β-sheets

ASJC Scopus subject areas

Ecology, Evolution, Behavior and Systematics
Space and Planetary Science

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10.1007/s11084-011-9257-y

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abstract = "Most self-replicating peptide systems are made of α-helix forming sequences. However, it has been postulated that shorter and simpler peptides may also serve as templates for replication when arranged into well-defined structures. We describe here the design and characterization of new peptides that form soluble β-sheet aggregates that serve to significantly accelerate their ligation and self-replication. We then discuss the relevance of these phenomena to early molecular evolution, in light of additional functionality associated with β-sheet assemblies.",

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author = "Valery Bourbo and Maayan Matmor and Elina Shtelman and Boris Rubinov and Nurit Ashkenasy and Gonen Ashkenasy",

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AU - Bourbo, Valery

AU - Matmor, Maayan

AU - Shtelman, Elina

AU - Rubinov, Boris

AU - Ashkenasy, Nurit

AU - Ashkenasy, Gonen

N1 - Funding Information: Acknowledgements We thank Dr. Riky Cohen-Luria for her help. This research was supported by a grant from the European Research Council (ERC 259204).

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Y1 - 2011/12/1

N2 - Most self-replicating peptide systems are made of α-helix forming sequences. However, it has been postulated that shorter and simpler peptides may also serve as templates for replication when arranged into well-defined structures. We describe here the design and characterization of new peptides that form soluble β-sheet aggregates that serve to significantly accelerate their ligation and self-replication. We then discuss the relevance of these phenomena to early molecular evolution, in light of additional functionality associated with β-sheet assemblies.

AB - Most self-replicating peptide systems are made of α-helix forming sequences. However, it has been postulated that shorter and simpler peptides may also serve as templates for replication when arranged into well-defined structures. We describe here the design and characterization of new peptides that form soluble β-sheet aggregates that serve to significantly accelerate their ligation and self-replication. We then discuss the relevance of these phenomena to early molecular evolution, in light of additional functionality associated with β-sheet assemblies.

KW - Prebiotic peptides

KW - Self-replication

KW - β-sheets

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Self-assembly and Self-replication of Short Amphiphilic β-sheet Peptides

Abstract

Keywords

ASJC Scopus subject areas

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