دورية أكاديمية
Controlled adsorption of multiple bioactive proteins enables targeted mast cell nanotherapy.
العنوان: | Controlled adsorption of multiple bioactive proteins enables targeted mast cell nanotherapy. |
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المؤلفون: | Du F; Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA., Rische CH; Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA.; Department of Medicine, Division of Allergy and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA., Li Y; Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL, USA., Vincent MP; Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA., Krier-Burris RA; Department of Medicine, Division of Allergy and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA., Qian Y; Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA., Yuk SA; Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA., Almunif S; Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA., Bochner BS; Department of Medicine, Division of Allergy and Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA., Qiao B; Department of Materials Science and Engineering, Northwestern University, Evanston, IL, USA.; Department of Natural Sciences, Baruch College, City University of New York, New York, NY, USA., Scott EA; Department of Biomedical Engineering, Northwestern University, Evanston, IL, USA. evan.scott@northwestern.edu.; Simpson Querrey Institute, Northwestern University, Chicago, IL, USA. evan.scott@northwestern.edu.; Chemistry of Life Processes Institute, Northwestern University, Evanston, IL, USA. evan.scott@northwestern.edu.; Interdisciplinary Biological Sciences Program, Northwestern University, Evanston, IL, USA. evan.scott@northwestern.edu.; Robert H. Lurie Comprehensive Cancer Center, Northwestern University, Chicago, IL, USA. evan.scott@northwestern.edu.; Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA. evan.scott@northwestern.edu. |
المصدر: | Nature nanotechnology [Nat Nanotechnol] 2024 May; Vol. 19 (5), pp. 698-704. Date of Electronic Publication: 2024 Jan 16. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101283273 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1748-3395 (Electronic) Linking ISSN: 17483387 NLM ISO Abbreviation: Nat Nanotechnol Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: London : Nature Pub. Group, 2006- |
مواضيع طبية MeSH: | Mast Cells*/drug effects , Mast Cells*/metabolism , Nanoparticles*/chemistry, Animals ; Mice ; Adsorption ; Humans ; Nanomedicine/methods ; Anaphylaxis ; Polypropylenes/chemistry ; Cell Degranulation/drug effects |
مستخلص: | Protein adsorption onto nanomaterials often results in denaturation and loss of bioactivity. Controlling the adsorption process to maintain the protein structure and function has potential for a range of applications. Here we report that self-assembled poly(propylene sulfone) (PPSU) nanoparticles support the controlled formation of multicomponent enzyme and antibody coatings and maintain their bioactivity. Simulations indicate that hydrophobic patches on protein surfaces induce a site-specific dipole relaxation of PPSU assemblies to non-covalently anchor the proteins without disrupting the protein hydrogen bonding or structure. As a proof of concept, a nanotherapy employing multiple mast-cell-targeted antibodies for preventing anaphylaxis is demonstrated in a humanized mouse model. PPSU nanoparticles displaying an optimized ratio of co-adsorbed anti-Siglec-6 and anti-FcεRIα antibodies effectively inhibit mast cell activation and degranulation, preventing anaphylaxis. Protein immobilization on PPSU surfaces provides a simple and rapid platform for the development of targeted protein nanomedicines. (© 2024. The Author(s), under exclusive licence to Springer Nature Limited.) |
التعليقات: | Update of: Res Sq. 2023 Jan 26;:. (PMID: 36747749) |
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معلومات مُعتمدة: | U19 AI136443 United States AI NIAID NIH HHS; DMR-0520547 National Science Foundation (NSF); R01 EB030629 United States EB NIBIB NIH HHS; R21 AI159586 United States AI NIAID NIH HHS; R21AI159586 U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID); R01EB030629 U.S. Department of Health & Human Services | NIH | National Institute of Biomedical Imaging and Bioengineering (NIBIB) |
تواريخ الأحداث: | Date Created: 20240116 Date Completed: 20240520 Latest Revision: 20240522 |
رمز التحديث: | 20240522 |
مُعرف محوري في PubMed: | PMC11105988 |
DOI: | 10.1038/s41565-023-01584-z |
PMID: | 38228804 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1748-3395 |
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DOI: | 10.1038/s41565-023-01584-z |