Abstract

Non-sericin (NS) extract was produced from the ethanolic extract of Bombyx mori silk cocoons. This extract is composed of both carotenoids and flavonoids. Many of these compounds are composed of substances of poor aqueous solubility. Thus, this study focused on the development of a carrier system created from biocompatible and biodegradable materials to improve the biological activity of NS extracts. Accordingly, NS was incorporated into human serum albumin template particles with MnCO3 (NS-HSA MPs) by loading NS into the preformed HAS-MnCO3 microparticles using the coprecipitation crosslinking dissolution technique (CCD-technique). After crosslinking and template dissolution steps, the NS loaded HSA particles are negatively charged, have a size ranging from 0.8 to 0.9 µm, and are peanut shaped. The degree of encapsulation efficiency ranged from 7% to 57% depending on the initial NS concentration and the steps of adsorption. In addition, NS-HSA MPs were taken up by human lung adenocarcinoma (A549 cell) for 24 h. The promotion of cellular uptake was evaluated by flow cytometry and the results produced 99% fluorescent stained cells. Moreover, the results from CLSM and 3D fluorescence imaging confirmed particle localization in the cells. Interestingly, NS-HSA MPs could not induce inflammation through nitric oxide production from macrophage RAW264.7 cells. This is the first study involving the loading of non-sericin extracts into HSA MPs by CCD technique to enhance the bioavailability and biological effects of NS. Therefore, HSA MPs could be utilized as a carrier system for hydrophobic substances targeting cells with albumin receptors.

Highlights

  • Silkworm (Bombyx mori) is an important insect of great economic significance in the textile industry

  • After dissolution the particle template, the final particle suspension of NS-Human serum albumin (HSA) MPs exhibited a yellow color as compared to the white color of Human Serum Albumin Micro Particles (HSA-MPs) that were used as a control

  • This entrapment was attributed due to hydrophobic interactions that occur between lipophilic substances of non-sericin components with the N-H functional group of albumin proteins

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Summary

Introduction

Silkworm (Bombyx mori) is an important insect of great economic significance in the textile industry. The biological activities of the sericin mixture are a result of the presence of sericin proteins or a combined effect of the non-sericin components. The natural coloring of a silk cocoon occurs on the surface of the sericin layer, which is dependent upon the strain of the B. mori silkworm [3]. A variety of cocoon shell colors may appear as a result of certain substances found in mulberry tree strains that occur during the feeding of B. mori larvae [6]. Biological functions, such as antioxidant activity and antityrosinase activity, have been studied in terms of their non-sericin components [7]. It is necessary to develop a carrier system to challenge their insolubility and to improve the biological effects of these non-sericin components for broader applications and usage

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