Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/87915
Type: Artigo de periódico
Title: Solid Lipid Nanoparticles For Hydrophilic Biotech Drugs: Optimization And Cell Viability Studies (caco-2 & Hepg-2 Cell Lines)
Author: Severino P.
Andreani T.
Jager A.
Chaud M.V.
Santana M.H.A.
Silva A.M.
Souto E.B.
Abstract: Insulin was used as model protein to developed innovative Solid Lipid Nanoparticles (SLNs) for the delivery of hydrophilic biotech drugs, with potential use in medicinal chemistry. SLNs were prepared by double emulsion with the purpose of promoting stability and enhancing the protein bioavailability. Softisan®100 was selected as solid lipid matrix. The surfactants (Tween®80, Span®80 and Lipoid®S75) and insulin were chosen applying a 22 factorial design with triplicate of central point, evaluating the influence of dependents variables as polydispersity index (PI), mean particle size (z-AVE), zeta potential (ZP) and encapsulation efficiency (EE) by factorial design using the ANOVA test. Therefore, thermodynamic stability, polymorphism and matrix crystallinity were checked by Differential Scanning Calorimetry (DSC) and Wide Angle X-ray Diffraction (WAXD), whereas the effect of toxicity of SLNs was check in HepG2 and Caco-2 cells. Results showed a mean particle size (z-AVE) width between 294.6 nm and 627.0 nm, a PI in the range of 0.425-0.750, ZP about -3 mV, and the EE between 38.39% and 81.20%. After tempering the bulk lipid (mimicking the end process of production), the lipid showed amorphous characteristics, with a melting point of ca. 30 °C. The toxicity of SLNs was evaluated in two distinct cell lines (HEPG-2 and Caco-2), showing to be dependent on the concentration of particles in HEPG-2 cells, while no toxicity in was reported in Caco-2 cells. SLNs were stable for 24 h in in vitro human serum albumin (HSA) solution. The resulting SLNs fabricated by double emulsion may provide a promising approach for administration of protein therapeutics and antigens. © 2014 Published by Elsevier Masson SAS.
Editor: Elsevier Masson SAS
Rights: fechado
Identifier DOI: 10.1016/j.ejmech.2014.04.084
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84900395929&partnerID=40&md5=7785ed77bbf26f6f7104b50eb4309ffd
Date Issue: 2014
Appears in Collections:Unicamp - Artigos e Outros Documentos

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