Trehalose lyophilisation stress-down of an albumin based nanoparticle to preserve structure/function

SIRI MACARENA; GRASSELLI MARIANO; ALONSO SILVIA DEL V.

Salto

Congreso; VII Poslatam and Latin American Crosstalk in Biophysics and Physiology. SBF.uy-SAB 2015; 2015

The aim of this study was to preserve albumin nanoparticle structure/function during thelyophilisation process. Bovine serum albumin nanoparticles were obtained by ­irradiation and lyophilised in buffer or in miliQ water/ threalose solution. For that purpose,the preservation of structure/function of lyophilised water soluble albumin nanoparticles indifferent protocols was studied. The size and charge of the nanoparticles were testedafter lyophilisation by Light Scattering and Z Potential. The size range of the BSAnanoparticle lyophilised in BPS was between 20 and 400 nm, assembling in differentaggregates of the nanoparticle, and Z potential obtained was negative (­6.65 mV).Thosenanoparticles lyophilised with trehalose had a size range of 30­70 nm and a Z potential of­24.00 mVMerocyanine 540 was used as a probe to test the binding properties of the NPs afterlyophilisation. Results showed more affinity between BSA NP­Lyo­T and the probe thanthe observed with BSA NP.Considering SH groups, no difference were observed between BSA, BSA NP and BSANP­Lyo­T.BSA NP­Lyo showed an increase in the free SH groups.Results suggest that for an effective long­term storage method lyophilisation of thenanoparticle should be carried out in miliQ water and trehalose.