Accelerated self-assembly of filipin proteins and formation of hydrogels

Abstract

This study delineates the novel revelation that traditional Chinese medicine polysaccharides facilitate and expedite the intramolecular conformational alterations within filipin proteins, culminating in amplified β-fold content and self-assembly proclivity to generate hydrogels. Augmentation of assembly kinetics was achieved by pH or ethanol supplementation. The resultant self-assembled hydrogels exhibited homogenous pore size distribution, registering porosities consistently surpassing 95 ± 2.3%, effectively accommodating pharmaceutical payloads. Noteworthy characteristics included low water loss rates spanning between 15% and 25%, exceptional swelling behavior, a storage modulus (G') ranging from 68 to 283 Pa, and discernible mechanical robustness. Insights into the self-assembly mechanism were preliminarily explained via Fourier infrared, Raman spectroscopy and X-ray diffraction spectroscopy analyses. In-depth examinations, encompassing in-vitro release, degradation and biocompatibility, corroborated the hydrogel’s capacity for smooth drug release, sustained stability, absence of cytotoxicity and favorable biocompatibility. In conclusion, the self-assembled filipin protein hydrogels preserved polysaccharide activity to a heightened extent and enhanced drug adaptability by reducing the overall formulation volume. This innovation, we suggest, holds significant promise for applications in sustained drug release and in the realm of tissue engineering materials.