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

Siri, Macarena; Grasselli, Mariano; Alonso, Silvia del Valle

doi:10.1016/j.jpba.2016.04.037

Cited by 21 publications

(32 citation statements)

References 16 publications

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“…The size of the NP obtained was of 70 nm of diameter and a Z potential value of -25 mV confirming data previously reported [5].To further characterise the BSA NP, different microscopy techniques were used to observe the shape of the aggregates. According to T.E.M, the BSA NP has a spherical-like shape with a given mean diameter of 35 nm (Figure 2a-b).…”

Section: Structure Morphology and Sizesupporting

confidence: 86%

“…The following concentrations were calculated based on the BSA NP molecular weight (MW 148 MDa) obtained from TEM (spherical shaped NPs) and DLS nanoparticle size of 70 nm. The DLS and Z Potential measures were taken with 90 Plus/Bi-MAS particle size analyzer as in Siri et al 2016 [5].…”

Section: Nanoparticle Characterisationmentioning

confidence: 99%

“…BSA NP and BSA samples in miliQ aqueous solution were normalised to an absorbance of 0.371 for this experiment. Samples were lyophilised overnight in order to eliminate any trace of water for the experiment as described in Siri et al, 2016. Approximately 4 mg of each sample was placed in sample pan and submitted to a heating ramp from 30 °C to 920 °C at 10 °C min-1 in a thermogravimetric balance (TA Q500, TA Instruments, United States).…”

Section: Tgamentioning

confidence: 99%

“…Nanoparticles formed from BSA molecules (BSA NP) due to desolvation in an ethanol solution were then stabilised by γ irradiation [3][4] [5] (Figure 1a). After the preparation process, the NPs were separated by a size exclusion chromatography column (Sephadex G -200) into different populations according to the order of elution; those of a larger size eluted first, followed by the smaller population ( Figure 1b).…”

Section: Size Exclusion Chromatography and Sds Gel Electrophoresismentioning

confidence: 99%

“…The aggregation eases the tailoring into desirable functional size-stable NPs for in vivo penetration. The preparation methods in ethanol solution and lyophilisation of the BSA NP were published in previous works [3][4] [5]. In this structural study, we give a complete biophysical characterisation of the gamma-irradiated albumin-based nanoparticle, where DLS size and microscopy was covered before [4].…”

Section: Introductionmentioning

confidence: 99%

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Effect of structure in ionized albumin – based nanoparticle: Characterisation, Emodin interaction, and in vitro cytotoxicity

Siri

Ruocco

Achilli

et al. 2019

Preprint

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A γ-irradiated bovine albumin serum based nanoparticle was characterised structurally, and functionally. The nanoparticle was characterised by A.F.M, D.L.S, zeta potential, T.E.M., gelelectrophoresis, spectroscopy (UV-Vis, Fluorescence, FT-IR, and CD). Its stability was studied under adverse experimental conditions: pH values, chaotropic agents, and ionic strength and stability studies against time were mainly carried out by fluorescence spectroscopy following the changes in the tryptophan environment in the nanoparticle. Its function was studied by the interaction of the NP with the hydrophobic drug Emodin was studied. The binding and kinetic properties of the obtained complex were tested by biophysical methods as well as its toxicity in tumour cells.According to its biophysics, the nanoparticle is a spherical nanosized vehicle with a hydrodynamic diameter of 70 nm. Data obtained describe the nanoparticle alone as nontoxic for cancer cell lines. When combined with Emodin, the bioconjugate proved to be more active on MCF-7 and PC-3 cancer cell lines than the nanoparticle alone. No haemolytic activity was found when tested against ex vivo red blood cells. The stability of the albumin nanoparticle is based on a competition between short-range attraction forces and long-range repulsion forces. The nanoparticle showed similar behaviour as albumin against pH while improving its stability in urea and tween 80. It was stable up to 15 days and presented no protein degradation in solutions up to 2 M salt concentration. Significantly, the albumin aggregate preserves the main activity-function of albumin and improved characteristics as an excellent carrier of molecules.

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Section: Structure Morphology and Sizesupporting

confidence: 86%

Section: Nanoparticle Characterisationmentioning

confidence: 99%

Section: Tgamentioning

confidence: 99%

Section: Size Exclusion Chromatography and Sds Gel Electrophoresismentioning

confidence: 99%