ArticleAngewandte Chemie (International ed. in English)2023
Side-Chain Chemistry Governs Hierarchical Order of Charge-Complementary β-sheet Peptide Coassemblies.
Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Charge Directed Selective Co-Assembly of Ionic Complementary Peptide Binary Mixtures.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Amyloid-ID: photocatalytic profiling of amyloid deposits in Alzheimer's disease tissue.Nature communications · 2026Article
- Complementary biomolecular coassemblies direct energy transport for cardiac photostimulators.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Harnessing Amino Acid Modularity for Programmable Function in Covalent Peptide Assemblies.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Molecular-Level Design Principles and Strategies of Peptide Self-Assembly Nanomaterials: From Sequence Engineering to Functional Applications.International journal of nanomedicine · 2025Review
- A Matter of Charge: Electrostatically Tuned Coassembly of Amphiphilic Peptides.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Supramolecular assembly of multifunctional protein gels via anMolecular systems design & engineering · 2024Article
- Programming co-assembled peptide nanofiber morphology via anionic amino acid type: Insights from molecular dynamics simulations.PLoS computational biology · 2023Article
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Authors and funding
11 authors.
Funding
Abstract
Self-assembly of proteinaceous biomolecules into functional materials with ordered structures that span length scales is common in nature yet remains a challenge with designer peptides under ambient conditions. This report demonstrates how charged side-chain chemistry affects the hierarchical co-assembly of a family of charge-complementary β-sheet-forming peptide pairs known as CATCH(X+/Y-) at physiologic pH and ionic strength in water. In a concentration-dependent manner, the CATCH(6K+) (Ac-KQKFKFKFKQK-Am) and CATCH(6D-) (Ac-DQDFDFDFDQD-Am) pair formed either β-sheet-rich microspheres or β-sheet-rich gels with a micron-scale plate-like morphology, which were not observed with other CATCH(X+/Y-) pairs. This hierarchical order was disrupted by replacing D with E, which increased fibril twisting. Replacing K with R, or mutating the N- and C-terminal amino acids in CATCH(6K+) and CATCH(6D-) to Qs, increased observed co-assembly kinetics, which also disrupted hierarchical order. Due to the ambient assembly conditions, active CATCH(6K+)-green fluorescent protein fusions could be incorporated into the β-sheet plates and microspheres formed by the CATCH(6K+/6D-) pair, demonstrating the potential to endow functionality.
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