ArticlePLoS computational biology2023
Programming co-assembled peptide nanofiber morphology via anionic amino acid type: Insights from molecular dynamics simulations.
Article in PLoS computational biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- In silico peptide self-assembly reveals the importance of N-terminal motifs and the inhibition mechanism of the mutation L38M in α-synuclein fibrillation.Protein science : a publication of the Protein Society · 2026Article
- Interplay of Hydrophobicity, Charge, and Sequence Length in Oligopeptide Coassembly.The journal of physical chemistry. B · 2025Article
- A Matter of Charge: Electrostatically Tuned Coassembly of Amphiphilic Peptides.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- 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
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Authors and funding
5 authors.
Funding
Abstract
Co-assembling peptides can be crafted into supramolecular biomaterials for use in biotechnological applications, such as cell culture scaffolds, drug delivery, biosensors, and tissue engineering. Peptide co-assembly refers to the spontaneous organization of two different peptides into a supramolecular architecture. Here we use molecular dynamics simulations to quantify the effect of anionic amino acid type on co-assembly dynamics and nanofiber structure in binary CATCH(+/-) peptide systems. CATCH peptide sequences follow a general pattern: CQCFCFCFCQC, where all C's are either a positively charged or a negatively charged amino acid. Specifically, we investigate the effect of substituting aspartic acid residues for the glutamic acid residues in the established CATCH(6E-) molecule, while keeping CATCH(6K+) unchanged. Our results show that structures consisting of CATCH(6K+) and CATCH(6D-) form flatter β-sheets, have stronger interactions between charged residues on opposing β-sheet faces, and have slower co-assembly kinetics than structures consisting of CATCH(6K+) and CATCH(6E-). Knowledge of the effect of sidechain type on assembly dynamics and fibrillar structure can help guide the development of advanced biomaterials and grant insight into sequence-to-structure relationships.
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