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Stabilization of Fibronectin by Random Copolymer Brushes Inhibits Macrophage Activation

  • David Faulón Marruecos
    David Faulón Marruecos
    Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States
  • Leila S. Saleh
    Leila S. Saleh
    Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States
  • Hye Hyun Kim
    Hye Hyun Kim
    Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States
    More by Hye Hyun Kim
  • Stephanie J. Bryant
    Stephanie J. Bryant
    Department of Chemical and Biological Engineering,  BioFrontiers Institute  and  Material Science and Engineering Program, University of Colorado, Boulder, Colorado 80309, United States
  • Daniel K. Schwartz*
    Daniel K. Schwartz
    Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States
    *Mailing Address: Daniel K. Schwartz, University of Colorado Boulder, Department of Chemical and Biological Engineering, Campus Box 596, Boulder, Colorado 80309, United States; Tel: (303) 735-0240; Fax: (303) 492-4341; E-mail: [email protected]
  • , and 
  • Joel L. Kaar*
    Joel L. Kaar
    Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States
    *Mailing Address: Joel L. Kaar, University of Colorado Boulder, Department of Chemical and Biological Engineering, Campus Box 596, Boulder, Colorado 80309, United States; Tel: (303) 492-6031; Fax: (303) 492-4341; E-mail: [email protected]
    More by Joel L. Kaar
Cite this: ACS Appl. Bio Mater. 2019, 2, 11, 4698–4702
Publication Date (Web):October 31, 2019
https://doi.org/10.1021/acsabm.9b00815
Copyright © 2019 American Chemical Society

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    Supporting Info (4)»

    Abstract

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    We show that protein unfolding on biomaterials may be dramatically reduced via tuning the chemical heterogeneity of the protein–material interface. Specifically, using dynamic single-molecule methods, we confirmed that the transient structure and dynamics of fibronectin (FN) may be mediated through varying the composition of random copolymer brushes. The brushes, which themselves represent an intriguing biomaterial, were composed of oligoethylene glycol and sulfobetaine methacrylate and presumably stabilized FN through partitioning and/or segregation of the copolymers. We further showed that, by controlling the transient structure and dynamics of FN, the secretion of TNF-α and IL-6 by RAW 264.7 was markedly diminished.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acsabm.9b00815.

    • Experimental details, image processing and data analysis, and supporting tables and figures (PDF)

    • Description of Movies S1 and S2 (PDF)

    • Raw data from SM-FRET experiment of labeled FNIII 8–10 molecules in contact with 75% SBMA/25% OEGMA surface (MP4)

    • Raw data from SM-FRET experiment of labeled FNIII 8–10 molecules in contact with 100% OEGMA surface (MP4)

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    Cited By

    This article is cited by 15 publications.

    1. Samuel A. Blackman, Dalton Miles, Joshita Suresh, Sarah Calve, Stephanie J. Bryant. Cell- and Serum-Derived Proteins Act as DAMPs to Activate RAW 264.7 Macrophage-like Cells on Silicone Implants. ACS Biomaterials Science & Engineering 2024, 10 (3) , 1418-1434. https://doi.org/10.1021/acsbiomaterials.3c01393
    2. Roger Chang, Martin Gruebele, Deborah E. Leckband. Protein Folding Stability and Kinetics in Alginate Hydrogels. Biomacromolecules 2023, 24 (11) , 5245-5254. https://doi.org/10.1021/acs.biomac.3c00764
    3. Héctor Sánchez-Morán, Luciana Rocha Barros Gonçalves, Daniel K. Schwartz, Joel L. Kaar. Framework for Optimizing Polymeric Supports for Immobilized Biocatalysts by Computational Analysis of Enzyme Surface Hydrophobicity. ACS Catalysis 2023, 13 (7) , 4304-4315. https://doi.org/10.1021/acscatal.3c00264
    4. Eugenie Jumai’an, Lechuan Zhang, Michael A. Bevan. Blood Protein Exclusion from Polymer Brushes. ACS Nano 2023, 17 (3) , 2378-2386. https://doi.org/10.1021/acsnano.2c09332
    5. Héctor Sánchez-Morán, James S. Weltz, Daniel K. Schwartz, Joel L. Kaar. Understanding Design Rules for Optimizing the Interface between Immobilized Enzymes and Random Copolymer Brushes. ACS Applied Materials & Interfaces 2021, 13 (23) , 26694-26703. https://doi.org/10.1021/acsami.1c02443
    6. Andres F. Chaparro Sosa, Riley M. Bednar, Ryan A. Mehl, Daniel K. Schwartz, Joel L. Kaar. Faster Surface Ligation Reactions Improve Immobilized Enzyme Structure and Activity. Journal of the American Chemical Society 2021, 143 (18) , 7154-7163. https://doi.org/10.1021/jacs.1c02375
    7. Bing Chen, Yuan Wang, Yang Guo, Peng Shi, Feng Wang. NaYbF4@NaYF4 Nanoparticles: Controlled Shell Growth and Shape-Dependent Cellular Uptake. ACS Applied Materials & Interfaces 2021, 13 (2) , 2327-2335. https://doi.org/10.1021/acsami.0c20757
    8. Leila S. Saleh, Casey Vanderheyden, Andrew Frederickson, Stephanie J. Bryant. Prostaglandin E2 and Its Receptor EP2 Modulate Macrophage Activation and Fusion in Vitro. ACS Biomaterials Science & Engineering 2020, 6 (5) , 2668-2681. https://doi.org/10.1021/acsbiomaterials.9b01180
    9. Héctor Sánchez-Morán, Joel L. Kaar, Daniel K. Schwartz. Supra-biological performance of immobilized enzymes enabled by chaperone-like specific non-covalent interactions. Nature Communications 2024, 15 (1) https://doi.org/10.1038/s41467-024-46719-5
    10. Berke Çalbaş, Ashley N. Keobounnam, Christopher Korban, Ainsley Jade Doratan, Tiffany Jean, Aryan Yashvardhan Sharma, Thaiesha A. Wright. Protein–polymer bioconjugation, immobilization, and encapsulation: a comparative review towards applicability, functionality, activity, and stability. Biomaterials Science 2024, 99 https://doi.org/10.1039/D3BM01861J
    11. Ghazal Bashiri, Marshall S. Padilla, Kelsey L. Swingle, Sarah J. Shepherd, Michael J. Mitchell, Karin Wang. Nanoparticle protein corona: from structure and function to therapeutic targeting. Lab on a Chip 2023, 23 (6) , 1432-1466. https://doi.org/10.1039/D2LC00799A
    12. Victoria T. Reichelderfer, Andres F. Chaparro Sosa, Joel L. Kaar, Daniel K. Schwartz. Tuning the surface charge of phospholipid bilayers inhibits insulin fibrilization. Colloids and Surfaces B: Biointerfaces 2022, 220 , 112904. https://doi.org/10.1016/j.colsurfb.2022.112904
    13. Syeda Tajin Ahmed, Deborah E. Leckband. Forces between mica and end-grafted statistical copolymers of sulfobetaine and oligoethylene glycol in aqueous electrolyte solutions. Journal of Colloid and Interface Science 2022, 608 , 1857-1867. https://doi.org/10.1016/j.jcis.2021.09.175
    14. Edna Johana Bolívar-Monsalve, Mario Moisés Alvarez, Samira Hosseini, Michelle Alejandra Espinosa-Hernandez, Carlos Fernando Ceballos-González, Margarita Sanchez-Dominguez, Su Ryon Shin, Berivan Cecen, Shabir Hassan, Ernesto Di Maio, Grissel Trujillo-de Santiago. Engineering bioactive synthetic polymers for biomedical applications: a review with emphasis on tissue engineering and controlled release. Materials Advances 2021, 2 (14) , 4447-4478. https://doi.org/10.1039/D1MA00092F
    15. Alexander H. Jesmer, Ryan G. Wylie. Controlling Experimental Parameters to Improve Characterization of Biomaterial Fouling. Frontiers in Chemistry 2020, 8 https://doi.org/10.3389/fchem.2020.604236

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