ArticleProceedings of the National Academy of Sciences of the United States of America2013
Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 139 citations in OpenAlex.
- Article
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- Substitution of tyrosine with electron-deficient aromatic amino acids improves Ac-PHF6 self-assembly and hydrogelation.RSC advances · 2025Article
- Investigating the Interactions of Peptide Nucleic Acids with Multicomponent Peptide Hydrogels for the Advancement of Healthcare Technologies.Gels (Basel, Switzerland) · 2025Article
- 2D Interfacial Crystallization Stabilized by Short-Chain Aliphatic Interfaces.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Biostable hydrogels consisting of hybrid β-sheet fibrils assembled by a pair of enantiomeric peptides.Materials today. Bio · 2024Article
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- Fabrication of a three-dimensional bone marrow niche-like acute myeloid Leukemia disease model by an automated and controlled process using a robotic multicellular bioprinting system.Biomaterials research · 2023Article
- Fabrication of lumen-forming colorectal cancer organoids using a newly designed laminin-derived bioink.International journal of bioprinting · 2023Article
- Acidic pH Promotes Refolding and Macroscopic Assembly of Amyloid β (16-22) Peptides at the Air-Water Interface.The journal of physical chemistry letters · 2022Article
- Fibril Structure Demonstrates the Role of Iodine Labelling on a Pentapeptide Self-Assembly.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Wall-free droplet microfluidics for probing biological processes by high-brilliance X-ray scattering techniques.Frontiers in molecular biosciences · 2022Review
- Directed Assembly of Multi-Walled Nanotubes and Nanoribbons of Amino Acid Amphiphiles Using a Layer-by-Layer Approach.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Fibrillation of Human Calcitonin and Its Analogs: Effects of Phosphorylation and Disulfide Reduction.Biophysical journal · 2021Article
- "What Doesn't Kill You Makes You Stronger": Future Applications of Amyloid Aggregates in Biomedicine.Molecules (Basel, Switzerland) · 2020Review
- Sequence-Dependent Nanofiber Structures of Phenylalanine and Isoleucine Tripeptides.International journal of molecular sciences · 2020Article
- Biomimetic peptide self-assembly for functional materials.Nature reviews. Chemistry · 2020Article
- Molecular design principles of Lysine-DOPA wet adhesion.Nature communications · 2020Article
- Ultrashort Peptide Self-Assembly: Front-Runners to Transport Drug and Gene Cargos.Frontiers in bioengineering and biotechnology · 2020Review
- Nanostructures Formed by Custom-Made Peptides Based on Amyloid Peptide Sequences and Their Inhibition by 2-Hydroxynaphthoquinone.Frontiers in chemistry · 2020Article
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The self-assembly of abnormally folded proteins into amyloid fibrils is a hallmark of many debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders and diabetes type II. However, the fundamental mechanism of amyloid aggregation remains poorly understood. Core sequences of four to seven amino acids within natural amyloid proteins that form toxic fibrils have been used to study amyloidogenesis. We recently reported a class of systematically designed ultrasmall peptides that self-assemble in water into cross-β-type fibers. Here we compare the self-assembly of these peptides with natural core sequences. These include core segments from Alzheimer's amyloid-β, human amylin, and calcitonin. We analyzed the self-assembly process using circular dichroism, electron microscopy, X-ray diffraction, rheology, and molecular dynamics simulations. We found that the designed aliphatic peptides exhibited a similar self-assembly mechanism to several natural sequences, with formation of α-helical intermediates being a common feature. Interestingly, the self-assembly of a second core sequence from amyloid-β, containing the diphenylalanine motif, was distinctly different from all other examined sequences. The diphenylalanine-containing sequence formed β-sheet aggregates without going through the α-helical intermediate step, giving a unique fiber-diffraction pattern and simulation structure. Based on these results, we propose a simplified aliphatic model system to study amyloidosis. Our results provide vital insight into the nature of early intermediates formed and suggest that aromatic interactions are not as important in amyloid formation as previously postulated. This information is necessary for developing therapeutic drugs that inhibit and control amyloid formation.
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