ArticleACS nano2017
Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils.
Article in ACS nano, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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Who cites it
22 citing papers in PubMed, 57 citations in OpenAlex.
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- Uncovering supramolecular chirality codes for the design of tunable biomaterials.Nature communications · 2024Article
- TMEM106B core deposition associates with TDP-43 pathology and is increased in risk SNP carriers for frontotemporal dementia.Science translational medicine · 2024Article
- Discovery, validation, and prodrug design of an ACE2 activator for treating bacterial infection-induced lung inflammation.Journal of controlled release : official journal of the Controlled Release Society · 2023Article
- Mapping the configurational landscape and aggregation phase behavior of the tau protein fragment PHF6.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Biomimetic Sequence-Templating Approach toward a Multiscale Modulation of Chromogenic Polymer Properties.Macromolecules · 2023Article
- Structural Remodeling Mechanism of the Toxic Amyloid Fibrillary Mediated by Epigallocatechin-3-gallate.ACS omega · 2022Article
- Collagen-Binding Peptide-Enabled Supramolecular Hydrogel Design for Improved Organ Adhesion and Sprayable Therapeutic Delivery.Nano letters · 2022Article
- Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges.International journal of molecular sciences · 2021Review
- Dual Control of Peptide Conformation with Light and Metal Coordination.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from MedinJournal of the American Chemical Society · 2020Article
- Combined Tumor Environment Triggered Self-Assembling Peptide Nanofibers and Inducible Multivalent Ligand Display for Cancer Cell Targeting with Enhanced Sensitivity and Specificity.Small (Weinheim an der Bergstrasse, Germany) · 2020Article
- Modular design and self-assembly of multidomain peptides towards cytocompatible supramolecular cell penetrating nanofibers.RSC advances · 2020Article
- Coassembly-Induced Transformation of Dipeptide Amyloid-Like Structures into Stimuli-Responsive Supramolecular Materials.ACS nano · 2020Article
- Direct Identification of Amyloid Peptide Fragments in Human α-Synuclein Based on Consecutive Hydrophobic Amino Acids.ACS omega · 2020Article
- Protein Supramolecular Structures: From Self-Assembly to Nanovaccine Design.Nanomaterials (Basel, Switzerland) · 2020Review
- Sequence isomerism-dependent self-assembly of glycopeptide mimetics with switchable antibiofilm properties.Chemical science · 2019Article
- Amyloid Fibril Design: Limiting Structural Polymorphism in Alzheimer's Aβ Protofilaments.The journal of physical chemistry. B · 2018Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
Abstract
Determining the structural origins of amyloid fibrillation is essential for understanding both the pathology of amyloidosis and the rational design of inhibitors to prevent or reverse amyloid formation. In this work, the decisive roles of peptide structures on amyloid self-assembly and morphological diversity were investigated by the design of eight amyloidogenic peptides derived from islet amyloid polypeptide. Among the segments, two distinct morphologies were highlighted in the form of twisted and planar (untwisted) ribbons with varied diameters, thicknesses, and lengths. In particular, transformation of amyloid fibrils from twisted ribbons into untwisted structures was triggered by substitution of the C-terminal serine with threonine, where the side chain methyl group was responsible for the distinct morphological change. This effect was confirmed following serine substitution with alanine and valine and was ascribed to the restriction of intersheet torsional strain through the increased hydrophobic interactions and hydrogen bonding. We also studied the variation of fibril morphology (i.e., association and helicity) and peptide aggregation propensity by increasing the hydrophobicity of the peptide side group, capping the N-terminus, and extending sequence length. We anticipate that our insights into sequence-dependent fibrillation and morphological diversity will shed light on the structural interpretation of amyloidogenesis and development of structure-specific imaging agents and aggregation 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.