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  • Physical and biological characterization of sericin-loaded copolymer liposomes stabilized by polyvinyl alcohol.

Physical and biological characterization of sericin-loaded copolymer liposomes stabilized by polyvinyl alcohol.

Colloids and surfaces. B, Biointerfaces (2016-11-05)
Kunat Suktham, Thongchai Koobkokkruad, Somsak Saesoo, Nattika Saengkrit, Suvimol Surassmo
ABSTRACT

Sericin protein (SP) is widely used as a nutrient biomaterial for biomedical and cosmeceutical applications although it shows low stability to heat and light. To overcome these problems and add value to wastewater from the silk industry, sericin protein was recovered as sericin-loaded copolymer-liposomes (SP-PVA-LP), prepared through thin film hydration. The size and morphology of the liposomes were investigated using dynamic light scattering (DLS), and electron microscopy (SEM and TEM). The particle size, liposome surface morphology and encapsulation efficiency of SP were dependent on PVA concentration. The hydrodynamic size of the nanoparticles was between 200 and 400nm, with the degree of negative charge contingent on sericin loading. SEM and TEM images confirmed the mono-dispersity, and spherical nature of the particles, with FTIR measurements confirming the presence of surface bound PVA. Exposure of liposomes to 500ppm sericin highlighted a dependence of encapsulation efficiency on PVA content; 2% surface PVA proved the optimal level for sericin loading. Cytotoxicity and viability assays revealed that SP-loaded surface modified liposomes promote cellular attachment and proliferation of human skin fibroblasts without adverse toxic effects. Surface modified copolymer liposomes show high performance in maintaining structural stability, and promoting enhancements in the solubility and bio-viability of sericin. Taken together, these biocompatible constructs allow for effective controlled release, augmenting sericin activity and resulting in effective drug delivery systems.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Sericin Bombyx mori (silkworm)