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Mesoporous silica particles as potential carriers for protein drug delivery: protein immobilisation and the effect of displacer on γ-globulin release

Mesoporous silica particles as potential carriers for protein drug delivery: protein immobilisation and the effect of displacer on γ-globulin release

Ajiboye, Adejumoke Lara, Trivedi, Vivek and Mitchell, John ORCID: 0000-0003-2945-3292 (2020) Mesoporous silica particles as potential carriers for protein drug delivery: protein immobilisation and the effect of displacer on γ-globulin release. Drug Development and Industrial Pharmacy, Drug Development and Industrial Pharmacy, 46 (4). pp. 576-586. ISSN 0363-9045 (Print), 1520-5762 (Online) (doi:https://doi.org/10.1080/03639045.2020.1742141)

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Abstract

The adsorption of γ-globulin was evaluated with experiments with silica particles marketed as Syloid AL1-FP (SAL), XDP-3150 (SXDP), and 244FP (SFP). The influence of pH, pore sizes, and degree of surface porosity on the extent of γ-globulin immobilisation was examined. Protein adsorption on these particles was largely related to their surface porosity and pore sizes. The adsorption capacity was established to be greater with mesoporous SFP and SXDP particles at 474 and 377 mg/g respectively when compared to significantly low-porosity SAL (16 mg/g). Additionally, γ-globulin immobilisation was favoured at pH closer to iso-electric point. A key aim of this work was to better understand and improve the limited reversibility of protein adsorption. Protein desorption was found to be lower in simulated intestinal fluid (SIF) in comparison to pH 7.4 phosphate buffer (PB). The use of displacer molecules [sodium dodecyl sulphate (SDS)/tween80/pluronic F127 (PF127)] promoted protein desorption from the adsorbent surface by the exchange mechanism. The PF127 provided substantial release in both studied condition but the highest release of 83% of γ-globulin from SXDP was obtained with tween 80 in PB. The released protein was analysed with circular dichroism (CD) spectroscopy which indicated that the secondary structure of desorbed γ-globulin was dependent on the pH and displacer molecule. The conformation largely remained unchanged when desorption was carried out in SIF but changed markedly in PB specially in the presence of SDS.

Item Type: Article
Uncontrolled Keywords: Mesoporous silica particles, carriers for protein drug delivery, protein immobilisation, γ-globulin release
Subjects: R Medicine > RS Pharmacy and materia medica
Faculty / School / Research Centre / Research Group: Faculty of Engineering & Science
Faculty of Engineering & Science > Medway Centre for Pharmaceutical Science
Faculty of Engineering & Science > School of Science (SCI)
Last Modified: 12 Mar 2021 01:38
URI: http://gala.gre.ac.uk/id/eprint/27425

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