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

Feoktistova, NA, Balabushevich, NG, Skirtach, AG, Volodkin, D ORCID: https://orcid.org/0000-0001-7474-5329 and Vikulina, AS, 2020. Inter-protein interactions govern protein loading into porous vaterite CaCO3 crystals. Physical Chemistry Chemical Physics, 22 (17), pp. 9713-9722. ISSN 1463-9076

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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.

Item Type:	Journal article
Publication Title:	Physical Chemistry Chemical Physics
Creators:	Feoktistova, N.A., Balabushevich, N.G., Skirtach, A.G., Volodkin, D. and Vikulina, A.S.
Publisher:	Royal Society of Chemistry
Date:	7 May 2020
Volume:	22
Number:	17
ISSN:	1463-9076
Identifiers:	Number Type 10.1039/d0cp00404a DOI 1347135 Other
Rights:	© The Owner Societies 2020. Open Access Article. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
Divisions:	Schools > School of Science and Technology
Record created by:	Jill Tomkinson
Date Added:	29 Jul 2020 14:37
Last Modified:	07 Feb 2022 14:49
URI:	https://irep.ntu.ac.uk/id/eprint/40294

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