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Inter-protein interactions govern protein loading into porous vaterite CaCO3 crystals

(2020) PHYSICAL CHEMISTRY CHEMICAL PHYSICS. 22(17). p.9713-9722
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Abstract
The fast development of protein therapeutics has resulted in a high demand for advanced delivery carriers that can effectively host therapeutic proteins, preserve their bioactivity and release them on demand. Accordingly, vaterite CaCO3 crystals have attracted special attention as sacrificial templates for protein encapsulation in micro- and nanoparticles (capsules and beads, respectively) under mild biofriendly conditions. This study aimed to better understand the mechanism of protein loading into crystals as a primary step for protein encapsulation. The loading of three therapeutic proteins (250 kDa catalase, 5.8 kDa insulin, and 6.5 kDa aprotinin) was investigated for crystals with different porosities. However, unexpectedly, the protein loading capacity was not consistent with the protein molecular weight. It solely depends on the inter-protein interactions in the bulk solution in the presence of crystals and that inside the crystals. The smallest protein aprotinin aggregates in the bulk (its aggregate size is about 100 nm), which prohibits its loading into the crystals. Insulin forms hexamers in the bulk, which can diffuse into the crystal pores but tend to aggregate inside the pores, suppressing protein diffusion inward. Catalase, the largest protein tested, does not form any aggregates in the bulk and diffuses freely into the crystals; however, its diffusion into small pores is sterically restricted. These findings are essential for the encapsulation of protein therapeutics by means of templating based on CaCO3 crystals and for the engineering of protein-containing microparticles having desired architectures.
Keywords
Enzymes, encapsulation, activity, calcium carbonate, catalysis, CALCIUM-CARBONATE, MICROPARTICLES, DELIVERY, ADSORPTION, GROWTH, MICROSPHERES, CAPSULES, NANOPARTICLES, ENCAPSULATION, CAPABILITIES

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MLA
Feoktistova, Natalia A., et al. “Inter-Protein Interactions Govern Protein Loading into Porous Vaterite CaCO3 Crystals.” PHYSICAL CHEMISTRY CHEMICAL PHYSICS, vol. 22, no. 17, 2020, pp. 9713–22, doi:10.1039/d0cp00404a.
APA
Feoktistova, N. A., Balabushevich, N. G., Skirtach, A., Volodkin, D., & Vikulina, A. S. (2020). Inter-protein interactions govern protein loading into porous vaterite CaCO3 crystals. PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 22(17), 9713–9722. https://doi.org/10.1039/d0cp00404a
Chicago author-date
Feoktistova, Natalia A., Nadezhda G. Balabushevich, Andre Skirtach, Dmitry Volodkin, and Anna S. Vikulina. 2020. “Inter-Protein Interactions Govern Protein Loading into Porous Vaterite CaCO3 Crystals.” PHYSICAL CHEMISTRY CHEMICAL PHYSICS 22 (17): 9713–22. https://doi.org/10.1039/d0cp00404a.
Chicago author-date (all authors)
Feoktistova, Natalia A., Nadezhda G. Balabushevich, Andre Skirtach, Dmitry Volodkin, and Anna S. Vikulina. 2020. “Inter-Protein Interactions Govern Protein Loading into Porous Vaterite CaCO3 Crystals.” PHYSICAL CHEMISTRY CHEMICAL PHYSICS 22 (17): 9713–9722. doi:10.1039/d0cp00404a.
Vancouver
1.
Feoktistova NA, Balabushevich NG, Skirtach A, Volodkin D, Vikulina AS. Inter-protein interactions govern protein loading into porous vaterite CaCO3 crystals. PHYSICAL CHEMISTRY CHEMICAL PHYSICS. 2020;22(17):9713–22.
IEEE
[1]
N. A. Feoktistova, N. G. Balabushevich, A. Skirtach, D. Volodkin, and A. S. Vikulina, “Inter-protein interactions govern protein loading into porous vaterite CaCO3 crystals,” PHYSICAL CHEMISTRY CHEMICAL PHYSICS, vol. 22, no. 17, pp. 9713–9722, 2020.
@article{8667993,
  abstract     = {The fast development of protein therapeutics has resulted in a high demand for advanced delivery carriers that can effectively host therapeutic proteins, preserve their bioactivity and release them on demand. Accordingly, vaterite CaCO3 crystals have attracted special attention as sacrificial templates for protein encapsulation in micro- and nanoparticles (capsules and beads, respectively) under mild biofriendly conditions. This study aimed to better understand the mechanism of protein loading into crystals as a primary step for protein encapsulation. The loading of three therapeutic proteins (250 kDa catalase, 5.8 kDa insulin, and 6.5 kDa aprotinin) was investigated for crystals with different porosities. However, unexpectedly, the protein loading capacity was not consistent with the protein molecular weight. It solely depends on the inter-protein interactions in the bulk solution in the presence of crystals and that inside the crystals. The smallest protein aprotinin aggregates in the bulk (its aggregate size is about 100 nm), which prohibits its loading into the crystals. Insulin forms hexamers in the bulk, which can diffuse into the crystal pores but tend to aggregate inside the pores, suppressing protein diffusion inward. Catalase, the largest protein tested, does not form any aggregates in the bulk and diffuses freely into the crystals; however, its diffusion into small pores is sterically restricted. These findings are essential for the encapsulation of protein therapeutics by means of templating based on CaCO3 crystals and for the engineering of protein-containing microparticles having desired architectures.},
  author       = {Feoktistova, Natalia A. and Balabushevich, Nadezhda G. and Skirtach, Andre and Volodkin, Dmitry and Vikulina, Anna S.},
  issn         = {1463-9076},
  journal      = {PHYSICAL CHEMISTRY CHEMICAL PHYSICS},
  keywords     = {Enzymes,encapsulation,activity,calcium carbonate,catalysis,CALCIUM-CARBONATE,MICROPARTICLES,DELIVERY,ADSORPTION,GROWTH,MICROSPHERES,CAPSULES,NANOPARTICLES,ENCAPSULATION,CAPABILITIES},
  language     = {eng},
  number       = {17},
  pages        = {9713--9722},
  title        = {Inter-protein interactions govern protein loading into porous vaterite CaCO3 crystals},
  url          = {http://dx.doi.org/10.1039/d0cp00404a},
  volume       = {22},
  year         = {2020},
}

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