ReviewPrion
Self assembly of short aromatic peptides into amyloid fibrils and related nanostructures.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- Unveiling the multifaceted potential of amyloid fibrils: from pathogenic myths to biotechnological marvels.Biophysical reviews · 2024Review
- 3,4-Ethylenedioxythiophene Hydrogels: Relating Structure and Charge Transport in Supramolecular Gels.Chemistry of materials : a publication of the American Chemical Society · 2024Article
- Essential Role of Histidine for Rapid Copper(II)-Mediated Disassembly of Neurokinin B Amyloid.Biomolecules · 2022Article
- Fibril Structure Demonstrates the Role of Iodine Labelling on a Pentapeptide Self-Assembly.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Peptide Self-Assembled Nanostructures: From Models to Therapeutic Peptides.Nanomaterials (Basel, Switzerland) · 2022Review
- Prediction of Transmembrane Regions, Cholesterol, and Ganglioside Binding Sites in Amyloid-Forming Proteins Indicate Potential for Amyloid Pore Formation.Frontiers in molecular neuroscience · 2021Article
- Exploiting Peptide Self-Assembly for the Development of Minimalistic Viral Mimetics.Frontiers in chemistry · 2021Review
- Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information.Frontiers in bioengineering and biotechnology · 2021Review
- Biomimetic peptide self-assembly for functional materials.Nature reviews. Chemistry · 2020Article
- Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities.Nature communications · 2020Article
- Article
- ZnScientific reports · 2018Article
- Thermodynamics of Amyloid-β Fibril Elongation: Atomistic Details of the Transition State.ACS chemical neuroscience · 2018Article
- Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils.ACS nano · 2017Article
- New route for self-assembly of α-lactalbumin nanotubes and their use as templates to grow silver nanotubes.PloS one · 2017Article
- Self-assembly of a nine-residue amyloid-forming peptide fragment of SARS corona virus E-protein: mechanism of self aggregation and amyloid-inhibition of hIAPP.Biochemistry · 2015Article
- Functionalization of α-synuclein fibrils.Beilstein journal of nanotechnology · 2015Article
- The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2014Article
- More than meets the eye: conformational switching of a stacked dialkoxynaphthalene-naphthalenetetracarboxylic diimide (DAN-NDI) foldamer to an NDI-NDI fibril aggregate.Chemistry (Weinheim an der Bergstrasse, Germany) · 2013Article
- Modulation of the cannabinoid receptors by hemopressin peptides.Life sciences · 2013Review
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of amyloid fibrils is the hallmark of more than twenty human disorders of unrelated etiology. In all these cases, ordered fibrillar protein assemblies with a diameter of 7-10 nm are being observed. In spite of the great clinical important of amyloid-associated diseases, the molecular recognition and self-assembly processes that lead to the formation of the fibrils are not fully understood. One direction to decipher the mechanism of amyloid formation is the use of short peptides fragments as model systems. Short peptide fragments, as short as pentapeptides, were shown to form typical amyloid assemblies in vitro that have ultrastructural, biophysical, and cytotoxic properties, as those of assemblies that are being formed by full length polypeptides. When we analyzed such short fragments, we identified the central role of aromatic moieties in the ability to aggregate into ordered nano-fibrillar structures. This notion allowed us to discover additional very short amyloidogenic peptides as well as other aromatic peptide motifs, which can form various assemblies at the nano-scale (including nanotubes, nanospheres, and macroscopic hydrogels with nano-scale order). Other practical utilization of this concept, together with novel beta breakage methods, is their use for the development of novel classes of amyloid formation inhibitors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.