ArticleACS central science2020
Unbiased Identification of the Liposome Protein Corona using Photoaffinity-based Chemoproteomics.
Article in ACS central science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The trial behind it
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
30 citing papers in PubMed.
- Multidimensional Protein Corona Analysis Toward Predictive Nano-Bio Interface Design.Small methods · 2026Review
- The protein corona at the nano-bio interface: the need for standardized methodology and opportunities for neurodegenerative disease intervention.RSC advances · 2026Review
- Planar Lipid Bilayers and Liposomes: Essential Models for Advancing Protein Structure and Function Research.Advances in experimental medicine and biology · 2026Review
- Review
- Protein corona formed on lipid nanoparticles compromises delivery efficiency of mRNA cargo.Nature communications · 2025Article
- Therapeutic Implications of Biomolecular Corona on Lipid Nanoparticle-Based Gene Delivery Systems.Small science · 2025Article
- Defining STING-sterol interactions with chemoproteomics.RSC chemical biology · 2025Article
- Emerging Approaches for Studying Lipid Dynamics, Metabolism, and Interactions in Cells.Annual review of biochemistry · 2025Review
- New fluorogenic triacylglycerols as sensors for dynamic measurement of lipid oxidation.Analytical and bioanalytical chemistry · 2025Article
- Small molecule modulation of protein corona for deep plasma proteome profiling.Nature communications · 2024Article
- Protein Corona of Nanoparticles: Isolation and Analysis.Chem & bio engineering · 2024Review
- Deep Plasma Proteome Profiling by Modulating Single Nanoparticle Protein Corona with Small Molecules.bioRxiv : the preprint server for biology · 2024Article
- Review
- Liposomes-Encapsulating Double-Stranded Nucleic Acid (Poly I:C) for Head and Neck Cancer Treatment.ACS pharmacology & translational science · 2024Article
- Article
- A magnetic separation method for isolating and characterizing the biomolecular corona of lipid nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Chemical Approaches for Measuring and Manipulating Lipids at the Organelle Level.Cold Spring Harbor perspectives in biology · 2023Review
- 'Passive' nanoparticles for organ-selective systemic delivery: design, mechanism and perspective.Chemical Society reviews · 2023Review
- Phase-Separated Liposomes Hijack Endogenous Lipoprotein Transport and Metabolism Pathways to Target Subsets of Endothelial Cells In Vivo.Advanced healthcare materials · 2023Article
- The protein corona from nanomedicine to environmental science.Nature reviews. Materials · 2023Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein adsorption to the surface of a nanoparticle can fundamentally alter the character, behavior, and fate of a nanoparticle in vivo. Current methods to capture the protein corona rely on physical separation techniques and are unable to resolve key, individual protein-nanoparticle interactions. As a result, the precise link between the "synthetic" and the "biological" identity of a nanoparticle remains unclear. Herein, we report an unbiased photoaffinity-based approach to capture, characterize, and quantify the protein corona of liposomes in their native state. Compared to conventional methods, our photoaffinity approach reveals markedly different interacting proteins as well as reduced total protein binding to liposome surfaces. Identified proteins do not follow protein abundancy patterns of human serum, as has been generally reported, but are instead dominated by soluble apolipoproteins-endogenous serum proteins that have evolved to recognize the lipidic surface of circulating lipoproteins. We believe our findings are the most accurate characterization of a liposome's biological identity but, more fundamentally, reveal liposome-protein binding is, in many cases, significantly less complex than previously thought.
Identifiers
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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.