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Lihi Adler-Abramovich

Researcher at Tel Aviv University

Publications -  122
Citations -  7175

Lihi Adler-Abramovich is an academic researcher from Tel Aviv University. The author has contributed to research in topics: Diphenylalanine & Self-healing hydrogels. The author has an hindex of 39, co-authored 107 publications receiving 5760 citations. Previous affiliations of Lihi Adler-Abramovich include University of Cyprus & Technion – Israel Institute of Technology.

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The physical properties of supramolecular peptide assemblies: from building block association to technological applications.

TL;DR: The use of peptide nanostructures was indeed recently demonstrated in various fields including the design of molecular motors based on nanostructure complexation with a metal-organic framework, the delivery of therapeutic agents, the development of energy storage devices and the fabrication of piezoelectric-based sensors.
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Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures.

TL;DR: This work finds that the averaged point stiffness of the nanotubes is 160 N/m, and that they have a correspondingly high Young's modulus of approximately 19 GPa, as calculated by finite element analysis.
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Self-assembled arrays of peptide nanotubes by vapour deposition

TL;DR: This work demonstrates the self-assembly of large arrays of aromatic peptide nanotubes using vapour deposition methods and shows that the nanotube arrays can be used to develop high-surface-area electrodes for energy storage applications, highly hydrophobic self-cleaning surfaces and microfluidic chips.
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Thermal and Chemical Stability of Diphenylalanine Peptide Nanotubes: Implications for Nanotechnological Applications

TL;DR: The significant thermal and chemical stability of the peptide nanotubes demonstrated here points toward their possible use in conventional microelectronic and microelectromechanics processes and fabrication into functional nanotechnological devices.
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Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

TL;DR: It is demonstrated that at pathological concentrations, phenylalanine self-assembles into fibrils with amyloid-like morphology and well-ordered electron diffraction, suggesting a new amyloidsosis-like etiology for PKU.