ArticleNature communications2024
Influence of chirality and sequence in lysine-rich lipopeptide biosurfactants and micellar model colloid systems.
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.
What it found
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Who cites it
9 citing papers in PubMed.
- Self-Assembly of a Therapeutic Peptide Surfactant: A Small-Angle X-ray Scattering Study.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Bioinspired Self-Assembly-Reinforced Ion Transport and Interface Regulation Enables Sustainable Metal-Ion Batteries for Wearable Electronics.Nano-micro letters · 2026Article
- Elucidating β-Sheet Ordering in Lipopeptides Bearing Lysine-Rich Tripeptide Sequences: Fibrils versus Nanotapes.The journal of physical chemistry. B · 2026Article
- Small-angle scattering studies on diverse peptide-based nanotube and helical ribbon structures reveal distinct form and structure factors.Journal of applied crystallography · 2025Article
- Semaglutide Aggregates into Oligomeric Micelles and Short Fibrils in Aqueous Solution.Biomacromolecules · 2025Article
- Molecular Dynamics Simulations of Self-Assembled EACS physical chemistry Au · 2025Article
- Effect of Chirality and Amphiphilicity on the Antimicrobial Activity of Tripodal Lysine-Based Peptides.ACS applied bio materials · 2025Article
- Micellization of Lipopeptides Containing Toll-like Receptor Agonist and Integrin Binding Sequences.ACS applied materials & interfaces · 2024Review
- Chirality and pH Influence the Self-Assembly of Antimicrobial Lipopeptides with Diverse Nanostructures.ACS applied bio materials · 2024Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Lipopeptides can self-assemble into diverse nanostructures which can be programmed to incorporate peptide sequences to achieve a remarkable range of bioactivities. Here, the influence of peptide sequence and chirality on micelle structure and interactions is investigated in a series of lipopeptides bearing two lysine or D-lysine residues and tyrosine or tryptophan residues, attached to a hexadecyl lipid chain. All molecules self-assemble into micelles above a critical micelle concentration (CMC). Small-angle x-ray scattering (SAXS) is used to probe micelle shape and structure from the form factor and to probe inter-micellar interactions via analysis of structure factor. The CMC is obtained consistently from surface tension and electrical conductivity measurements. We introduce a method to obtain the zeta potential from the SAXS structure factor which is in good agreement with directly measured values. Atomistic molecular dynamics simulations provide insights into molecular packing and conformation within the lipopeptide micelles which constitute model self-assembling colloidal systems and biomaterials.
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Registered trials
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