Protein corona meets freeze-drying: overcoming the... - BV FAPESP
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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Protein corona meets freeze-drying: overcoming the challenges of colloidal stability, toxicity, and opsonin adsorption

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Author(s):
Picco, Agustin S. [1, 2] ; Mondo, Gabriela Borba [1, 3] ; Ferreira, Larissa Fernanda [1, 4] ; de Souza, Edmarcia Elisa [1] ; Peroni, Luis Antonio [5] ; Cardoso, Mateus Borba [1, 3, 4]
Total Authors: 6
Affiliation:
[1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Synchrotron Light Lab LNLS, BR-13083970 Campinas, SP - Brazil
[2] Univ Nacl La Plata, CONICET, Fac Cs Exactas, Inst Invest Fisicoquim Teor & Aplicadas INIFTA, Diagonal 113 & 64, RA-1900 La Plata - Argentina
[3] Univ Campinas UNICAMP, Inst Chem IQ, POB 6154, BR-13083970 Campinas, SP - Brazil
[4] Univ Fed ABC, Programa Posgrad Biotecnociencia, BR-09210580 Santo Andre, SP - Brazil
[5] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biosci Natl Lab LNBio, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 5
Document type: Journal article
Source: NANOSCALE; v. 13, n. 2, p. 753-762, JAN 14 2021.
Web of Science Citations: 0
Abstract

Freeze-drying of nanoparticle suspensions is capable of generating stable nanoformulations with improved storage times and easier transportation. Nonetheless, nanoparticle aggregation is likely induced during freeze-drying, which reduces its redispersibility upon reconstitution and leads to undesirable effects such as non-specific toxicity and impaired efficacy. In this work, bovine serum albumin (BSA) is described as a suitable protectant for silica nanoparticles (SNPs), which result in solid structures with excellent redispersibility and negligible signs of aggregation even when longer storage times are considered. We experimentally demonstrated that massive system aggregation can be prevented when a saturated BSA corona around the nanoparticle is formed before the lyophilization process. Furthermore, the BSA corona is able to suppress non-specific interactions between these nanoparticles and biological systems, as evidenced by the lack of residual cytotoxicity, hemolytic activity and opsonin adsorption. Hence, BSA can be seriously considered for industry as an additive for nanoparticle freeze-drying since it generates solid and redispersible nanoformulations with improved biocompatibility. (AU)

FAPESP's process: 17/02145-7 - Study of the interaction between proteins and functionalized silica nanoparticles
Grantee:Larissa Fernanda Ferreira
Support Opportunities: Scholarships in Brazil - Master
FAPESP's process: 14/22322-2 - Functionalization of silica nanoparticles: increasing biological interaction
Grantee:Mateus Borba Cardoso
Support Opportunities: Regular Research Grants
FAPESP's process: 15/25406-5 - Organizing matter: colloids formed by association of surfactants, polymers and nanoparticles
Grantee:Watson Loh
Support Opportunities: Research Projects - Thematic Grants