Binding of PFOS to serum albumin and DNA: insight into the molecular toxicity of perfluorochemicals

<p>Abstract</p> <p>Background</p> <p>Health risk from exposure of perfluorochemicals (PFCs) to wildlife and human has been a subject of great interest for understanding their molecular mechanism of toxicity. Although much work has been done, the toxigenicity of PFCs remains largely unknown. In this work, the non-covalent interactions between perfluorooctane sulfonate (PFOS) and serum albumin (SA) and DNA were investigated under normal physiological conditions, aiming to elucidate the toxigenicity of PFCs.</p> <p>Results</p> <p>In equilibrium dialysis assay, the bindings of PFOS to SA correspond to the Langmuir isothermal model with two-step sequence model. The saturation binding number of PFOS was 45 per molecule of SA and 1 per three base-pairs of DNA, respectively. ITC results showed that all the interactions were spontaneous driven by entropy change. Static quenching of the fluorescence of SA was observed when interacting with PFOS, indicating PFOS bound Trp residue of SA. CD spectra of SA and DNA changed obviously in the presence of PFOS. At normal physiological conditions, 1.2 mmol/l PFOS reduces the binding ratio of Vitamin B₂to SA by more than 30%.</p> <p>Conclusion</p> <p>The ion bond, van der Waals force and hydrophobic interaction contributed to PFOS binding to peptide chain of SA and to the groove bases of DNA duplex. The non-covalent interactions of PFOS with SA and DNA alter their secondary conformations, with the physiological function of SA to transport Vitamin B₂being inhibited consequently. This work provides a useful experimental method for further studying the toxigenicity of PFCs.</p

Synthesis of Carbide Lime Waste Derived Base Catalyst (KF/CLW-Fe3O4) for Methyl Ester Production: An Optimization Study

In this paper, solid base catalyst KF/CLW-Fe3O4 was prepared from carbide lime waste, primarily calcium hydroxide with tiny amounts of carbonate and; the catalyst was used in the optimization study on the methyl ester production. The new strong base catalyst was synthesized by chemical impregnation. This catalyst was characterized by Hammett indicator analysis, Brunauer, Emmett, and Teller (BET), scanning electron microscope (SEM), X-ray diffraction (XRD) and temperature-programmed desorption (TPD) of carbon dioxide. The catalyst was further used to catalyzed the transesterification reaction to produce methyl ester. Taguchi method was used to assess the impact of catalyst at different intervals of reaction parameters, including reaction time, methanol to oil ratio, and catalyst loading. A mixed level of orthogonal array design with L9, analysis of variance (ANOVA) and signal to noise ratio were used to determine parameters that significantly impact the palm oil transesterification reaction. High methyl ester conversion was attained, and the catalyst can be easily separated and reused. KF/CLW-Fe3O4 has great potential to be used to produce methyl ester because of its high catalytic activity and environmental friendliness. Copyright © 2021 by Authors, Published by BCREC Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).

Activation of the Extracellular Signal-Regulated Kinase Signaling Is Critical for Human Umbilical Cord Mesenchymal Stem Cell Osteogenic Differentiation

Human umbilical cord mesenchymal stem cells (hUCMSCs) are recognized as candidate progenitor cells for bone regeneration. However, the mechanism of hUCMSC osteogenesis remains unclear. In this study, we revealed that mitogen-activated protein kinases (MAPKs) signaling is involved in hUCMSC osteogenic differentiation in vitro. Particularly, the activation of c-Jun N-terminal kinases (JNK) and p38 signaling pathways maintained a consistent level in hUCMSCs through the entire 21-day osteogenic differentiation period. At the same time, the activation of extracellular signal-regulated kinases (ERK) signaling significantly increased from day 5, peaked at day 9, and declined thereafter. Moreover, gene profiling of osteogenic markers, alkaline phosphatase (ALP) activity measurement, and alizarin red staining demonstrated that the application of U0126, a specific inhibitor for ERK activation, completely prohibited hUCMSC osteogenic differentiation. However, when U0126 was removed from the culture at day 9, ERK activation and osteogenic differentiation of hUCMSCs were partially recovered. Together, these findings demonstrate that the activation of ERK signaling is essential for hUCMSC osteogenic differentiation, which points out the significance of ERK signaling pathway to regulate the osteogenic differentiation of hUCMSCs as an alternative cell source for bone tissue engineering. Copyright © 2016 Chen-Shuang Li et al

Proteomics study of serum exosomes in Kawasaki disease patients with coronary artery aneurysms

Background: To study the protein profile of the serum exosomes of patients with coronary artery aneurysms (CAA) caused by Kawasaki disease (KD). Methods: Two-dimensional electrophoresis (2-DE) was used to identify proteins from the exosomes of serum obtained from children with CAA caused by KD, as well as healthy controls. Differentially expressed proteins were identified using matrix-assisted laser desorption/ionization time-of-flight/timeof-flight mass spectrometry (MALDI-TOF/TOF MS) analysis. Results: Thirty two differentially expressed proteins were identified (18 up-regulated and 14 downregulated) from serum exosomes of children with CAA and were compared to healthy controls. The expression levels of 4 proteins (TN, RBP4, LRG1, and APOA4) were validated using Western blotting. Classification analysis and protein–protein network analysis showed that they are associated with multiple functional groups, including host immune response, inflammation, apoptotic process, developmental process, and biological adhesion process. Conclusions: These findings establish a comprehensive proteomic profile of serum exosomes from children with CAA caused by KD, and provide additional insights into the mechanisms of CAA caused by KD