Self-encapsulation and controlled release of recombinant proteins using novel silica-forming peptides as fusion linkers

• Published in: International journal of biological macromolecules Vol. 125; pp. 1175 - 1183
• Main Authors: Abdelhamid, Mohamed A.A., Yeo, Ki Baek, Ki, Mi-Ran, Pack, Seung Pil
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 15.03.2019
• Subjects: Amino Acid Sequence; Delayed-Action Preparations; Drug Compounding; Drug Liberation; Genes, Reporter; Nanoparticles - chemistry; Peptides - chemistry; Protein immobilization; Recombinant Fusion Proteins - administration & dosage; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - pharmacokinetics; Silica-forming peptide; Silicon Dioxide - chemistry; Spectrum Analysis; Sustained release; Protein immobilization; Sustained release; Silica-forming peptide
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2018.12.160

Recently, the potential use of biomimetic silica as smart matrices for the auto-encapsulation and controlled release of functional proteins has gained increased interest because of the mild synthesis conditions. Inspired by biological silicification, in this study, we studied novel silica-forming peptides (SFPs), Volp1 and Salp1, to mediate the generation of silica hybrids in vitro. The fusion of SFPs to model fluorescent proteins directed their auto-encapsulation in wet sol-gel silica materials. Furthermore, the SFPs served as affinity linkers for the immobilization of recombinant proteins in silica. Interestingly, the SFP fusion proteins modulated silicic acid polycondensation and allowed for the self-immobilization of SFP fusion proteins in two distinct silica formulations depending on the ionic strength—precipitated silica particles or wet silica gel. The controlled release of Salp1/Volp1 fusion proteins from silica matrices was significantly greater than that of the silaffin R5 fusion proteins. Subsequently, we showed that multiple SFP-tagged proteins homogenously entrapped within a silica matrix could be separately released following pre-incubation with different concentrations of l-arginine solution. These new findings provide a simple and reproducible route for silica hybrid formation for in situ stable auto-encapsulation and the sustained release of recombinant proteins with potential applications in biotechnology. [Display omitted] •Silica-based hybrid materials were prepared using novel silica forming peptides (SFPs), Volp1 and Salp1, as biocatalysts.•The SFPs served as affinity linkers for firmly immobilizing the recombinant proteins in silica materials.•The SFP fusion proteins accelerated the polymerization of silicic acid to form two distinct silica formulations.•SFPs had impact of improving the controlled release of their fusion proteins from silica matrices.•The multiple encapsulated proteins could be separately released from silica matrix.