ArticleAnalytical chemistry2019
Mapping Molecular Structure of Protein Locating on Nanoparticles with Limited Proteolysis.
Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed.
- Designing Functional Bionanoconstructs for EffectiveBioconjugate chemistry · 2022Review
- Biomolecular interactions of ultrasmall metallic nanoparticles and nanoclusters.Nanoscale advances · 2021Review
- Understanding How Staphylococcal Autolysin Domains Interact With Polystyrene Surfaces.Frontiers in microbiology · 2021Article
- Lipid and protein corona of food-grade TiONanoImpact · 2020Article
- A bispecific circular aptamer tethering a built-in universal molecular tag for functional protein delivery.Chemical science · 2020Article
- Disentangling Biomolecular Corona Interactions With Cell Receptors and Implications for Targeting of Nanomedicines.Frontiers in bioengineering and biotechnology · 2020Review
- Prediction of protein corona on nanomaterials by machine learning using novel descriptors.NanoImpact · 2020Article
- Engineered Polymeric Materials for Biological Applications: Overcoming Challenges of the Bio-Nano Interface.Polymers · 2019Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The molecular structure of a protein could be altered when it is attached to nanoparticles (NPs), affecting the performance of NPs present in biological systems. Limited proteolysis coupled with LC-MS/MS could reveal the changes in protein structure when it binds to a variety of entities, including macro-molecules and small drugs, but it has not yet been applied to study protein-NP interaction. Herein, adsorption of proteins, transferrin, and catalase on the polystyrene (PS) or iron oxide (IO) NPs was analyzed with this method. Both increased and decreased proteolytic efficiency in certain regions on the proteins were observed. Identification of the peptides affected by protein-NP interaction led to proper prediction of alterations to protein function as well as to colloidal stability of NPs. Overall, the present work has demonstrated the utility of limited proteolysis in helping to elucidate the potential biological outcomes of the protein-NP conjugate, obtaining knowledge to guide improvement of the rational design of the protein-conjugated NPs for biomedical applications and to understand the biological behaviors of the engineered NPs.
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Registered trials
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