Abstract
This research study attempts to prove the concept of the applicability of hyperthermia to treating the lysozyme amyloid fibrils (LAFs)’s self-assembled fibrillary aggregates by a feedback-modulated temperature controller ranging from 26 °C to 80 °C, and separately, by near-infrared (NIR) laser-irradiated cesium tungstate (CsWO3) nanoparticle (NPs). The dependence of the final morphology of the amyloidal assembly on external heating and the photothermal effect of the NPs on treating the fibrillary assembly were investigated and analyzed. Experimentally, atomic force microscopy (AFM), optical stereoscopy, and scanning electron microscopy (SEM) were used primarily to ensure mutual interaction between LAFs and NPs, optically elucidate the surface contour and final fibrillary assembly upon the influence of thermal treatment, and further reveal fine-details of the optical samples. Finally, conclusive remarks are drawn that the fibrillary structures doped with the NPs exhibit an increasing degree of unique orthogonality. As the temperature rises, utter deformation of the dendritic structures of fibrillary assemblies at 70 °C was found, and NIR laser-irradiated CsWO3 NPs have been demonstrated to be useful in topically destructing pre-assembled LAFs, which may be conducive to the future development of neurodegenerative therapeutic techniques.
Highlights
The assembly of amyloid fibrils of many protein origins is a potential cause of many life-threatening diseases [1]
This research aimed to optically elucidate the in vitro morphogenesis of the lysozyme fibrillary assembly incorporated with CsWO3 NPs, investigate the effect of external heating through direct increase of environmental temperature or the NIR laser-irradiated NPs on the lysozyme amyloid fibrils (LAFs) and nanocomposites, and assess the potential of the NPs on the treatment of the pre-assembled amyloidal fibrils
This research investigated, morphologically, the temperature-dependent morphogenesis of the self-assembled LAFs and nanocomposites doped with CsWO3 NPs and assessed the applicability of photothermal property of the NPs to treating the aggregates of LAFs
Summary
The assembly of amyloid fibrils of many protein origins is a potential cause of many life-threatening diseases [1]. A handful of aggregates of mutant versions of proteins—including tau protein [6], lysozyme [7], insulin [8], and hungtingtin [9]—have been found to be pathologically complicated with the degeneration of cerebral tissue, the dysfunction of visceral organs, the requirement of increased insulin intake for diabetic patients, and the cytotoxicity induced by abnormal expansion of CAG codon of glutamine (an α amino acid of hungtingtin) Such aggregating phenomena of the amyloidal polypeptides, either toxic or non-toxic, can occur both in vivo or in vitro [10] and have driven a plethora of investigative efforts into methods that prohibit, disintegrate, or destruct such amyloidal formations [11]. Despite the acquisition of electron microscopy images of lysozyme amyloid fibrils (LAFs) before and after the microwave irradiation was carried out, the dynamic process of such fibrillary disintegration due to the imposition of thermal energy is still lacking [24]
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