title: Albumin-based nanoparticle trehalose lyophilisation stress-down to preserve structure/function and enhanced binding.
abstract: The aim of this study was to preserve albumin nanoparticle structure/function during the lyophilisation process. Bovine serum albumin nanoparticles were obtained by γ-irradiation. Nanoparticles were lyophilised in buffer, miliQ water or in trehalose/miliQ solution. The size and charge of the nanoparticles were tested after lyophilisation by light scattering and Z potential. The most relevant results in size of BSA nanoparticle were those lyophilised in PBS between 20 and 350nm, assembled in different aggregates, and negative Z potential obtained was 37±8mV in all, and those nanoparticles lyophilised with trehalose had a size range of 70±2nm and a negative Z potential of 20±5mV. Structure determination of surface aminoacids SH groups in the BSA NP lyophilised in PBS showed an increase in the free SH groups. Different aggregates had different amount of SH groups exposure from 55 to 938 (from smaller to bigger aggregates), whereas BSA NP lyophilised with trehalose showed no significant difference if compared with BSA NP. The binding properties of the BSA nanoparticle with a theragnostic probe (merocyanine 540) were studied after lyophilisation. Results showed more affinity between the BSA NP lyophilised with trehalose than that observed with non lyophilised BSA NP. As a result, the lyophilisation condition in trehalose 100μM solution is the best one to preserve the BSA NP structure/function and the one with the enhance binding affinity of the BSA NP.
authors.affiliation: Laboratorio de Biomembranas (LBM), and GBEyB, Grupo Vinculado IMBICE-CONICET; Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Peña 352, Bernal, B1876BXD Buenos Aires, Argentina.
authors.forename: Macarena
authors.initials: M
authors.lastname: Siri
authors.affiliation: Laboratorio de Materiales Biotecnológicos (LaMaBio), and GBEyB, Grupo Vinculado IMBICE-CONICET; Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Peña 352, Bernal, B1876BXD Buenos Aires, Argentina.
authors.forename: Mariano
authors.initials: M
authors.lastname: Grasselli
authors.affiliation: Laboratorio de Biomembranas (LBM), and GBEyB, Grupo Vinculado IMBICE-CONICET; Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Peña 352, Bernal, B1876BXD Buenos Aires, Argentina. Electronic address: salonso@unq.edu.ar.
authors.forename: Silvia Del V
authors.initials: Sdel V
authors.lastname: Alonso
mesh_terms: D004337:Drug Carriers / Q000737:chemistry; D005456:Fluorescent Dyes / Q000008:administration & dosage; D005612:Freeze Drying; D053758:Nanoparticles; D010316:Particle Size; D011744:Pyrimidinones / Q000008:administration & dosage*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D014199:Trehalose / Q000737:chemistry*
chemical_list: D004337:Drug Carriers; D005456:Fluorescent Dyes; D011744:Pyrimidinones; D012710:Serum Albumin, Bovine; C003954:merocyanine dye; D014199:Trehalose
keywords: BSA nanoparticle; Dynamic light scattering; Lyophilisation; MC540 affinity-binding; Trehalose; Z potential