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    Protein Vesicles with pH-Responsive Disassembly
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    Biomacromolecules

    Cite this: Biomacromolecules 2022, 23, 9, 3678–3687
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    https://doi.org/10.1021/acs.biomac.2c00562
    Published August 9, 2022
    Copyright © 2022 American Chemical Society
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    Abstract

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    Protein biomaterials offer several advantages over those made from other components because their amino acid sequence can be precisely controlled with genetic engineering to produce a diverse set of material building blocks. In this work, three different elastin-like polypeptide (ELP) sequences were designed to synthesize pH-responsive protein vesicles. ELPs undergo a thermally induced hydrophobic transition that enables self-assembly of different kinds of protein biomaterials. The transition can be tuned by the composition of the guest residue, X, within the ELP pentapeptide repeat unit, VPGXG. When the guest residue is substituted with an ionizable amino acid, such as histidine, the ELP undergoes a pH-dependent hydrophobic phase transition. We used pH-responsive ELPs with different levels of histidine substitution, in combination with leucine zippers and globular, functional proteins, to fabricate protein vesicles. We demonstrate pH-dependent self-assembly, diameter, and disassembly of the vesicles using a combination of turbidimetry, dynamic light scattering, microscopy, and small angle X-ray scattering. As the ELP transition is dependent on the sequence, the vesicle properties also depend on the histidine content in the ELP building blocks. These results demonstrate the tunability of protein vesicles endowed with pH responsiveness, which expands their potential in drug-delivery applications.

    Copyright © 2022 American Chemical Society

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    • Epifluorescence images of mCherry-ZE/H5-ZR-ELP at pH 5.50 and 6.00, circular dichroism, SDS-PAGE gels of purified H-ZR-ELPs, size distributions of vesicles as a function of pH, and TEM images of vesicles (PDF)

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    This article is cited by 21 publications.

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    12. Diego López Barreiro, Abel Folch-Fortuny, Iain Muntz, Jens C. Thies, Cees M.J. Sagt, Gijsje H. Koenderink. Sequence Control of the Self-Assembly of Elastin-Like Polypeptides into Hydrogels with Bespoke Viscoelastic and Structural Properties. Biomacromolecules 2023, 24 (1) , 489-501. https://doi.org/10.1021/acs.biomac.2c01405
    13. Lan Yang, Qian-Yu Yuan, Ting-Ting Li, Ching-Wen Lou, Chun‐Yu Hung, Jia-Horng Lin. Recent developments and applications of pH-responsive polymers. Textile Research Journal 2025, 39 https://doi.org/10.1177/00405175241305543
    14. Yingying Zhang, Qi Zhao, Jingjiao Zhang, Shuo Wei, Fei Tao, Peng Yang. Bio‐Inspired Adaptive and Responsive Protein‐Based Materials. ChemPlusChem 2024, 89 (12) https://doi.org/10.1002/cplu.202400309
    15. Weiwei Wang, Yinfeng Wang, Zhenzhu Xia, Guijie Hao, Alex Tuffour, Lirong Yan, Jinping Chen, Yiying Zhu, Feng Lin, Yang Zhou. Enhancing the Purification and Stability of Superoxide Dismutase by Fusion with Thermoresponsive Self‐Assembly of Elastin Like Polypeptide. ChemistrySelect 2024, 9 (40) https://doi.org/10.1002/slct.202401100
    16. Chengyu Fu, Zhengge Wang, Xingyu Zhou, Bowen Hu, Chen Li, Peng Yang. Protein-based bioactive coatings: from nanoarchitectonics to applications. Chemical Society Reviews 2024, 53 (3) , 1514-1551. https://doi.org/10.1039/D3CS00786C
    17. Jooyong Shin, Yeongseon Jang. Rational design and engineering of polypeptide/protein vesicles for advanced biological applications. Journal of Materials Chemistry B 2023, 11 (37) , 8834-8847. https://doi.org/10.1039/D3TB01103H
    18. Yirui Li, Dylan R. Dautel, Mikaela A. Gray, Michael E. McKenna, Julie A. Champion. Rational design of elastin-like polypeptide fusion proteins to tune self-assembly and properties of protein vesicles. Journal of Materials Chemistry B 2023, 11 (27) , 6443-6452. https://doi.org/10.1039/D3TB00200D
    19. Jackson Powers, Yeongseon Jang. Temperature-responsive membrane permeability of recombinant fusion protein vesicles. Soft Matter 2023, 19 (18) , 3273-3280. https://doi.org/10.1039/D3SM00096F
    20. Elisabeth Garanger, Sébastien Lecommandoux. Emerging opportunities in bioconjugates of Elastin-like polypeptides with synthetic or natural polymers. Advanced Drug Delivery Reviews 2022, 191 , 114589. https://doi.org/10.1016/j.addr.2022.114589
    21. Yirui Li, Julie A. Champion. Self-assembling nanocarriers from engineered proteins: Design, functionalization, and application for drug delivery. Advanced Drug Delivery Reviews 2022, 189 , 114462. https://doi.org/10.1016/j.addr.2022.114462
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    Biomacromolecules

    Cite this: Biomacromolecules 2022, 23, 9, 3678–3687
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.biomac.2c00562
    Published August 9, 2022
    Copyright © 2022 American Chemical Society
    Request reuse permissions

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