The prolonged intake of the artificial sweetener aspartame is known to have deleterious effects. Our biophysical experimentations indicate that aspartame forms self-assembled fibrillar etiologies that affect the intrinsic integrity of...
The incorrect metabolic breakdown of the nonaromatic amino acid methionine (Met) leads to the disorder called hypermethioninemia via an unknown mechanism. To understand the molecular level pathogenesis of this disorder, we prepared a DMPC lipid membrane, the mimicking setup of the cell membrane, and explored the effect of the millimolar level of Met on it. We found that Met forms toxic fibrillar aggregates that disrupt the rigidity of the membrane bilayer, and increases the dynamic response of water molecules surrounding the membrane as well as the heterogeneity of the membrane. Such aggregates strongly deform red blood cells. This opens the requirement to consider therapeutic antagonists either to resist or to inhibit the toxic amyloid aggregates against hypermethioninemia. Moreover, such disrupting effect on membrane bilayer and cytotoxicity along with deformation effect on RBC by the cross amyloids of Met and Phenylalanine (Phe) was found to be most virulent. This exclusive observation of the enhanced virulent effect of the cross amyloids is expected to be an informative asset to explain the coexistence of two amyloid disorders.
One of the most common and leading cause of cancer death in human beings is lung cancer. The advanced observation of cancer takes the main role to inflate a patient's probability for survival of the disease. This paper inspects the accomplishment of support vector machine (SVM) and logistic regression (LR) algorithms in predicting the survival rate of lung cancer patients and compares the effectiveness of these two algorithms through accuracy, precision, recall, F1 score and confusion matrix. These techniques have been applied to detect the survival possibilities of lung cancer victims and help the physicians to take decisions on the forecast of the disease.
The naturally occurring yellow polyphenolic medicinal pigment curcumin shows ultrafast dynamics in the excited states. These ultrafast dynamics are strongly influenced by the rigidity of the environments of the systems. The present investigation unveils the ultrafast excited-state intramolecular hydrogen atom transfer (ESIHT) (which is involved in the antioxidant mechanism) and the solvation dynamics of curcumin inside the imidazolium surface active ionic liquid (SAIL), 1hexadecyl-3-methylimidazolium chloride ([C 16 mim]Cl) micelle, and giant vesicles after introducing sorbitan monoesters (Span 20 and Span 80) in the aqueous medium. Interestingly, the short hydrocarbon chain containing Span 20 forms smaller, less rigid vesicles, and the long hydrocarbon chain containing Span 80 forms larger, more rigid giant vesicles after being assembled with [C 16 mim]Cl. The ESIHT and the solvation dynamics are slower in Span 80, containing rigid vesicles, than that in Span 20, comprising less rigid vesicles. Finally, we have established a threecomponent fluorescence resonance energy transfer (Triple-FRET) system to generate white light (WL) in the micelle and giant vesicles. Here the hydrophobic dye 1,6-diphenyl-1,3,5-hexatriene (DPH) acts as the donor, and the hydrophilic anticancer drug doxorubicin hydrochloride (DOX) serves as the acceptor along with the intermediate donor, curcumin. At a specific combination of the concentrations of these dyes in a particular self-assembled system, WL is generated due to the triple-FRET phenomena.
Dopamine (DA) and 3,4-dihydroxy-L-phenylalanine (L-Dopa or DPA), a marker and medicine for the neurological disorder Parkinson's disease (PD), lead to the formation of polymeric fluorescent nanoparticles (F-Poly NPs or F-NPs or simply, NPs). The interaction study between proteins and NPs shows prominent interaction with strong specificity toward albumin type proteins for DPA derived and mixed NPs. Furthermore, encapsulation of the anticancer drug doxorubicin hydrochloride (Dox) inside the NP−protein conjugates results in excellent white light emission with pronounced specificity toward albumin proteins for F-PDPA and F-Mix NPs. Finally, the use of BSA protein fibril resulting in strong binding with NPs along with Dox assisted white light emission has also been studied.
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