ArticleNature communications2024
Chiral inversion induced by aromatic interactions in short peptide assembly.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Spectroscopic Insights into Lysozyme Structural Modulation by Polyphenols: A Combined FTIR and VCD Study.Molecules (Basel, Switzerland) · 2026Article
- Modulating Solvation Structure and Electrical Double Layer via Anion-Additive Weak Interactions for High-Voltage Lithium Metal Batteries.Angewandte Chemie (International ed. in English) · 2026Article
- Chirality induced by supramolecular self-assembly of fluorinated π-conjugated carbon dots for bright circularly polarized electroluminescent light-emitting diodes.Nature communications · 2026Article
- Elevational Variation in Rhizosphere Bacterial Assembly and Fine-Scale Taxon Differentiation ofMicroorganisms · 2026Article
- Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026Review
- Self-Assembly of Heterochiral and Homochiral Peptides Conjugated to PNA Dimers and Their Integration in Peptide-Based Hydrogels.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Chiroptical switching and strong circularly polarized luminescence in peptide supramolecular assemblies.Nature communications · 2025Article
- Chirality Effects in Peptide-Based Dynamic Combinatorial Chemistry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- 2D Interfacial Crystallization Stabilized by Short-Chain Aliphatic Interfaces.Langmuir : the ACS journal of surfaces and colloids · 2025Article
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Authors and funding
14 authors.
Funding
Abstract
Although hydrophobic interactions provide the main driving force for initial peptide aggregation, their role in regulating suprastructure handedness of higher-order architectures remains largely unknown. We here interrogate the effects of hydrophobic amino acids on handedness at various assembly stages of peptide amphiphiles. Our studies reveal that relative to aliphatic side chains, aromatic side chains set the twisting directions of single β-strands due to their strong steric repulsion to the backbone, and upon packing into multi-stranded β-sheets, the side-chain aromatic interactions between strands form the aromatic ladders with a directional preference. This ordering not only leads to parallel β-sheet arrangements but also induces the chiral flipping over of single β-strands within a β-sheet. In contrast, the lack of orientational hydrophobic interactions in the assembly of aliphatic peptides implies no chiral inversion upon packing into β-sheets. This study opens an avenue to harness peptide aggregates with targeted handedness via aromatic side-chain interactions.
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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.