Albumin-based nanoparticle trehalose lyophilisation stress-down to preserve structure/function and enhanced binding

MACARENA SIRI, MARIANO GRASSELLI AND SILVIA DEL VALLE ALONSO

JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2016

0731-7085

The aim of this study was to preserve albumin nanoparticle structure/function during the lyophilisation process. Bovine serum albumin nanoparticles were obtained by -irradiation. Nanoparticles were lyophilised inbuffer, 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 ofBSA nanoparticle were those lyophilised in PBS between 20 and 350 nm, assembled in different aggregates, and negative Z potential obtained was 37 ± 8 mV in all, and those nanoparticles lyophilised with trehalose had a size range of 70 ± 2 nm and a negative Z potential of 20 ± 5 mV. 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 showedmore affinity between the BSA NP lyophilised with trehalose than that observed with non lyophilised BSA NP. As a result, the lyophilisation condition in trehalose 100 µM solution is the best one to preserve the BSA NP structure/function and the one with the enhance binding affinity of the BSA NP. KEYWORDS: BSA nanoparticle, lyophilisation, trehalose, dynamic light scattering, Z potential, MC540 affinity-binding