ArticleNanoscale2017
Halogenation dictates the architecture of amyloid peptide nanostructures.
Article in Nanoscale, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Substituent-Based Modulation of Self-Assembly and Immunogenicity of Amphipathic Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Computation meets experiment: identification of highly efficient fibrillating peptides.CrystEngComm · 2023Article
- Impact of Reactive Species on Amino Acids-Biological Relevance in Proteins and Induced Pathologies.International journal of molecular sciences · 2022Review
- Fibril Structure Demonstrates the Role of Iodine Labelling on a Pentapeptide Self-Assembly.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Peptide-Protein Interactions: From Drug Design to Supramolecular Biomaterials.Molecules (Basel, Switzerland) · 2021Review
- Halogenation of theChemistryOpen · 2020Article
- Molecular dynamics investigation of halogenated amyloidogenic peptides.Journal of molecular modeling · 2019Article
- In Situ Generation of Chiroptically-Active Gold-Peptide Superstructures Promoted by Iodination.ACS nano · 2019Article
- A self-assembling peptide hydrogel for ultrarapid 3D bioassays.Nanoscale advances · 2019Article
- Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid peptides yield a plethora of interesting nanostructures though difficult to control. Here we report that depending on the number, position, and nature of the halogen atoms introduced into either one or both phenylalanine benzene rings of the amyloid β peptide-derived core-sequence KLVFF, four different architectures were obtained in a controlled manner. Our findings demonstrate that halogenation may develop as a general strategy to engineer amyloidal peptide self-assembly and obtain new amyloidal nanostructures.
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Registered trials
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