ArticleScientific reports2017
Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles.
Article in Scientific reports, 2017. 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.
- Valorization of Rapeseed Meal: Production, Fractionation, and Utilization Routes.Foods (Basel, Switzerland) · 2026Review
- Deep learning in the discovery of antiviral peptides and peptidomimetics: databases and prediction tools.Molecular diversity · 2025Review
- Caffeic Acid Phenethyl Ester Encapsulated in Self-Assemble Rice Peptides Nanoparticles: Storage Stability, In Vitro Release, and Their Interaction Mechanisms.Foods (Basel, Switzerland) · 2024Article
- Fragment-based drug nanoaggregation reveals drivers of self-assembly.Nature communications · 2023Article
- Stability of ACE2 Peptide Mimetics and Their Implications on the Application for SARS-CoV2 Detection.Biosensors · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amphipathic peptides are versatile building blocks for fabricating well-ordered nanostructures, which have gained much attention owing to their enormous design possibilities and bio-functionalities. However, using amphipathic peptides from natural proteins to create tunable nanostructures is challenging because of their heterogeneity and great tendency to form aggregates. Here we fabricated two well-defined nanoparticles from cruciferin amphipathic peptides by integrating top-down and bottom-up approach. Alkali hydrolysis (pH 12, 120 °C for 30 min) was introduced to break down intact cruciferin into peptides (top-down). The cruciferin peptides and their fractions were then assembled into nanoparticles (bottom-up) in the presence of calcium ions. The permeate fraction from 10 kDa cut-off membrane formed smaller nanoparticles (F1-NPs) (around 82 nm) than that of unfractionated cruciferin peptides (CRU-NPs, around 185 nm); the electrostatic and hydrophobic interactions were the main driving forces for particle formation. LC-MS/MS analysis characterised that the small amphipathic peptides (X
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Registered trials
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