ArticleProceedings of the National Academy of Sciences of the United States of America2020
Anatomy of a selectively coassembled β-sheet peptide nanofiber.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- Charge Directed Selective Co-Assembly of Ionic Complementary Peptide Binary Mixtures.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Highly sensitive chemiluminescence imaging of misfolded proteins in neurodegenerative models.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Probing Peptide Assembly and Interaction via High-Resolution Imaging Techniques: A Mini Review.International journal of molecular sciences · 2025Review
- A Matter of Charge: Electrostatically Tuned Coassembly of Amphiphilic Peptides.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Genetically Fusing Order-Promoting and Thermoresponsive Building Blocks to Design Hybrid Biomaterials.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Computational Design of Peptides for Biomaterials Applications.ACS applied bio materials · 2024Review
- Side-Chain Chemistry Governs Hierarchical Order of Charge-Complementary β-sheet Peptide Coassemblies.Angewandte Chemie (International ed. in English) · 2023Article
- Programming co-assembled peptide nanofiber morphology via anionic amino acid type: Insights from molecular dynamics simulations.PLoS computational biology · 2023Article
- Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering.Acta biomaterialia · 2022Review
- Peptide framework for screening the effects of amino acids on assembly.Science advances · 2022Article
- Advanced nanomaterial for prostate cancer theranostics.Frontiers in bioengineering and biotechnology · 2022Review
- Heterogeneous protein co-assemblies with tunable functional domain stoichiometry.Molecular systems design & engineering · 2022Article
- β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis.International journal of molecular sciences · 2021Review
- Catalytic amyloids: Is misfolding folding?Current opinion in chemical biology · 2021Review
- From structure to application: Progress and opportunities in peptide materials development.Current opinion in chemical biology · 2021Review
- De novo design of peptides that coassemble into β sheet-based nanofibrils.Science advances · 2021Article
- Glycosylation of a Nonfibrillizing Appendage Alters the Self-Assembly Pathway of a Synthetic β-Sheet Fibrillizing Peptide.The journal of physical chemistry. B · 2021Article
- Injectable nanofibrillar hydrogels based on charge-complementary peptide co-assemblies.Biomaterials science · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Peptide-Peptide Co-Assembly: A Design Strategy for Functional Detection of C-peptide, A Biomarker of Diabetic Neuropathy.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide self-assembly, wherein molecule A associates with other A molecules to form fibrillar β-sheet structures, is common in nature and widely used to fabricate synthetic biomaterials. Selective coassembly of peptide pairs A and B with complementary partial charges is gaining interest due to its potential for expanding the form and function of biomaterials that can be realized. It has been hypothesized that charge-complementary peptides organize into alternating ABAB-type arrangements within assembled β-sheets, but no direct molecular-level evidence exists to support this interpretation. We report a computational and experimental approach to characterize molecular-level organization of the established peptide pair, CATCH. Discontinuous molecular dynamics simulations predict that CATCH(+) and CATCH(-) peptides coassemble but do not self-assemble. Two-layer β-sheet amyloid structures predominate, but off-pathway β-barrel oligomers are also predicted. At low concentration, transmission electron microscopy and dynamic light scattering identified nonfibrillar ∼20-nm oligomers, while at high concentrations elongated fibers predominated. Thioflavin T fluorimetry estimates rapid and near-stoichiometric coassembly of CATCH(+) and CATCH(-) at concentrations ≥100 μM. Natural abundance
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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.