Abstract

Gelatin nanoparticles found numerous applications in drug delivery, bioimaging, immunotherapy, and vaccine development as well as in biotechnology and food science. Synthesis of gelatin nanoparticles is usually made by a two-step desolvation method, which, despite providing stable and homogeneous nanoparticles, has many limitations, namely complex procedure, low yields, and poor reproducibility of the first desolvation step. Herein, we present a modified one-step desolvation method, which enables the quick, simple, and reproducible synthesis of gelatin nanoparticles. Using the proposed method one can prepare gelatin nanoparticles from any type of gelatin with any bloom number, even with the lowest ones, which remains unattainable for the traditional two-step technique. The method relies on quick one-time addition of poor solvent (preferably isopropyl alcohol) to gelatin solution in the absence of stirring. We applied the modified desolvation method to synthesize nanoparticles from porcine, bovine, and fish gelatin with bloom values from 62 to 225 on the hundreds-of-milligram scale. Synthesized nanoparticles had average diameters between 130 and 190 nm and narrow size distribution. Yields of synthesis were 62–82% and can be further increased. Gelatin nanoparticles have good colloidal stability and withstand autoclaving. Moreover, they were non-toxic to human immune cells.

Highlights

  • We revealed that quick one-time addition of non-solvent to aqueous gelatin solution without agitation leads to the formation of monodisperse gelatin nanoparticles

  • In the course of preliminary experiments nanoparticles were successfully prepared from gelatin B with bloom values as low as 75

  • 25 kDa according to manufacturer). This result contradicts conclusions made by other researchers: usually, removal of low-molecular-weight gelatin fractions is necessary to obtain stable and fine nanoparticle suspensions [20,21]

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Summary

Introduction

Gelatin is a product of partial hydrolysis of collagen. In the course of gelatin preparation, collagen is pre-treated under acidic or alkaline conditions, which results in obtaining two types of gelatin: type A and type B, respectively. The main sources of gelatin are bovine skin, bovine hides, and cattle and pork bones, whereas fish and poultry gelatins are used to a limited extent [1]. Gelatin from cold-water fish contains a lower percentage of proline and hydroxyproline which are involved in the formation of collagen-like triple helices and has inferior gelation properties in comparison with mammalian gelatins [1,2]

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