Protein-Templated Biomimetic Silica Nanoparticles

• Published in: Langmuir Vol. 31; no. 12; pp. 3687 - 3695
• Main Authors: Jackson, Erienne, Ferrari, Mariana, Cuestas-Ayllon, Carlos, Fernández-Pacheco, Rodrigo, Perez-Carvajal, Javier, de la Fuente, Jesús M, Grazú, Valeria, Betancor, Lorena
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 31-03-2015
• Subjects: Animals; Biomimetic Materials - chemistry; Cattle; Chemical Phenomena; Nanoparticles - chemistry; Particle Size; Serum Albumin, Bovine - chemistry; Silicon Dioxide - chemistry; Surface Properties
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la504978r

Biomimetic silica particles can be synthesized as a nanosized material within minutes in a process mimicked from living organisms such as diatoms and sponges. In this work, we have studied the effect of bovine serum albumin (BSA) as a template to direct the synthesis of silica nanoparticles (NPs) with the potential to associate proteins on its surface. Our approach enables the formation of spheres with different physicochemical properties. Particles using BSA as a protein template were smaller (∼250–380 nm) and were more monodisperse than those lacking the proteic core (∼700–1000 nm) as seen by dynamic light scattering (DLS), scanning electron microscopy (SEM), and environmental scanning electron microscopy (ESEM) analysis. The absence of BSA during synthesis produced silica nanoparticles without any porosity that was detectable by nitrogen adsorption, whereas particles containing BSA developed porosity in the range of 4 to 5 nm which collapsed on the removal of BSA, thus producing smaller pores. These results were in accordance with the pore size calculated by high-resolution transmission electron microscopy (HTEM). The reproducibility of the BSA-templated nanoparticle properties was determined by analyzing four batches of independent synthesizing experiments that maintained their properties. The high positive superficial charge of the nanoparticles facilitated adsorption under mild conditions of a range of proteins from an E. coli extract and a commercial preparation of laccase from Trametes versicolor. All of the proteins were quantitatively desorbed. Experiments conducted showed the reusability of the particles as supports for the ionic adsorption of the biomolecules. The protein loading capacity of the BSA-based biomimetic particles was determined using laccase as 98.7 ± 6.6 mg·g–1 of particles.