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A comprehensive investigation of the interactions of human serum albumin with polymeric and hybrid nanoparticles

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Abstract

Nanoparticles (NPs) engineered as drug delivery systems continue to make breakthroughs as they offer numerous advantages over free therapeutics. However, the poor understanding of the interplay between the NPs and biomolecules, especially blood proteins, obstructs NP translation to clinics. Nano-bio interactions determine the NPs’ in vivo fate, efficacy and immunotoxicity, potentially altering protein function. To fulfill the growing need to investigate nano-bio interactions, this study provides a systematic understanding of two key aspects: (i) protein corona (PC) formation and (ii) NP-induced modifications on protein’s structure and stability. A methodology was developed by combining orthogonal techniques to analyze both quantitative and qualitative aspects of nano-bio interactions, using human serum albumin (HSA) as a model protein. Protein quantification via liquid chromatography-mass spectrometry, and capillary zone electrophoresis (CZE) clarified adsorbed protein quantity and stability. CZE further unveiled qualitative insights into HSA forms (native, glycated HSA and cysteinylated), while synchrotron radiation circular dichroism enabled analyzing HSA’s secondary structure and thermal stability. Comparative investigations of NP cores (organic vs. hybrid), and shells (with or without polyethylene glycol (PEG)) revealed pivotal factors influencing nano-bio interactions. Polymeric NPs based on poly(lactic-co-glycolic acid) (PLGA) and hybrid NPs based on metal-organic frameworks (nanoMOFs) presented distinct HSA adsorption profiles. PLGA NPs had protein-repelling properties while inducing structural modifications on HSA. In contrast, HSA exhibited a high affinity for nanoMOFs forming a PC altering thereby the protein structure. A shielding effect was gained through PEGylation for both types of NPs, avoiding the PC formation as well as the alteration of unbound HSA structure.

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All data and materials as well as software application or custom code support their published claims and comply with field standards. All data generated or analysed during this study are included in this published article.

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Acknowledgements

We thank Stéphanie Yen-Nicolaÿ from the Plateforme de Protéomique (Ingénierie et Plateformes au Service de l’Innovation Thérapeutique, Chatenay Malabry, France) for help with LC-MS investigations and fruitful discussions. SR-CD measurements on DISCO beamline at SOLEIL Synchrotron light source were performed under the proposals 20180883 and 20171494. We thank Matthieu REFREGIERS and Frank WIEN for welcoming us to the DISCO beamline.

Funding

This work is supported by a public grant overseen by the French National Research Agency (ANR) as part of the “Investissements d’Avenir” program (Labex NanoSaclay, reference: ANR-10-LABX-0035; Merve Seray Ural’s fellowship, reference ; ANR-11-IDEX-0003-02) and by ANR-20-CE19-0020.

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Authors and Affiliations

  1. Université Paris-Saclay, Institute of Molecular Sciences of Orsay, French National Center for Scientific Research, 91405, Orsay, France

    Merve Seray Ural, Joice Maria Joseph, Xue Li, My-An Tran & Ruxandra Gref

  2. Université Paris-Saclay, Institut Galien Paris-Saclay, French National Center for Scientific Research, 91400, Orsay, France

    Merve Seray Ural, Joice Maria Joseph, Myriam Taverna & Claire Smadja

  3. Synchrotron Soleil, 91190, Saint-Aubin, France

    Frank Wien

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Contributions

Conceived the study: RG, CS. Performed the experiments: MSU, JMJ, XL, MAT. Data treatment: MSU, JMJ, FW, CS, RG. Wrote the manuscript: MSU, CS, RG. Funding acquisition: RG, CS.

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Correspondence to Claire Smadja or Ruxandra Gref.

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Merve Seray Ural, Joice Maria Joseph, Frank Wien, Xue Li, My-An Tran, Myriam Taverna, Claire Smadja, Ruxandra Gref declare that they have no conflict of interest.

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Ural, M.S., Joseph, J.M., Wien, F. et al. A comprehensive investigation of the interactions of human serum albumin with polymeric and hybrid nanoparticles. Drug Deliv. and Transl. Res. (2024). https://doi.org/10.1007/s13346-024-01578-x

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