ACS Appl Mater Interfaces
November 2024
Aqueous zinc-ion batteries have been impeded by the hydrogen evolution reaction (HER), uncontrolled zinc dendrites, and side reactions on the Zn anode. In this work, a Zn-polyphenol supramolecular network is rationally designed for stabilizing Zn anodes (ZPN@Zn) even at high current density. Theoretical calculations and experiments show that the zinc-polyphenol supramolecular layer effectively inhibits the hydrogen evolution reaction by capturing water molecules through strong hydrogen bonding networks while also facilitating the rapid replenishment of Zn ions at the interface through supramolecular anchoring.
View Article and Find Full Text PDFBisphenol F (BPF), BPS and BPAF are gaining popularity as main substitutes to BPA, but there is no clear evidence that these compounds disrupt glycemic homeostasis in the same way. In this study, four bisphenols were administered to C57BL/6 J mice, and showed that the serum insulin was elevated in the BPA and BPS exposed mice, whereas BPF exposed mice exhibited lower serum insulin and higher blood glucose. BPF decreased oxidized glutathione/reduced glutathione ratio (GSSG/GSH) and N6-methyladenosine (m6A) levels, which was responsible for pancreatic apoptosis in mice.
View Article and Find Full Text PDFBackground/aims: Adhesion-regulating molecule 1 (ADRM1), a receptor located on the 26S proteasome, is upregulated in many solid cancers. However, little is known about its role in acute leukemia (AL).
Methods: We determined ADRM1 expression levels in both untreated AL samples and leukemia cell lines using real-time polymerase chain reaction or Western blot analysis.
Glycosylation has significant effects on protein function and cell metastasis, which are important in cancer progression. It is of great interest to identify site-specific glycosylation in search of potential cancer biomarkers. However, the abundance of glycopeptides is low compared to that of nonglycopeptides after trypsin digestion of serum samples, and the mass spectrometric signals of glycopeptides are often masked by coeluting nonglycopeptides due to low ionization efficiency.
View Article and Find Full Text PDFWe have developed herein a quantitative mass spectrometry-based approach to analyze the etiology-related alterations in fucosylation degree of serum haptoglobin in patients with liver cirrhosis and hepatocellular carcinoma (HCC). The three most common etiologies, including infection with hepatitis B virus (HBV), infection with hepatitis C virus (HCV), and heavy alcohol consumption (ALC), were investigated. Only 10 μL of serum was used in this assay in which haptoglobin was immunoprecipitated using a monoclonal antibody.
View Article and Find Full Text PDFA mass spectrometry-based methodology has been developed to study changes in core-fucosylation of serum ceruloplasmin that are site-specific between cirrhosis and hepatocellular carcinoma (HCC). The serum samples studied for these changes were from patients affected by cirrhosis or HCC with different etiologies, including alcohol, hepatitis B virus, or hepatitis C virus. The methods involved trypsin digestion of ceruloplasmin into peptides followed by Endo F3 digestion, which removed most of the glycan structure while retaining the innermost N-acetylglucosamine (GlcNAc) and/or core-fucose bound to the peptide.
View Article and Find Full Text PDFWe describe a label-free relative quantification LC-MS/MS method for core-fucosylation in alpha-2-macroglobulin (A2MG) immunoprecipitated from human sera. The method utilizes endoglycosidase F partial deglycosylation to reduce glycosylation microheterogeneity, while retaining the innermost N-acetylglucosamine (GlcNAc) and core fucose. Precursor ion peak areas of partially deglycosylated peptides were obtained and site-specific core-fucosylation ratios based on the peak areas of core-fucosylated and nonfucosylated counterparts were calculated and evaluated for assay development.
View Article and Find Full Text PDFProtein glycosylation plays an important role in multiple cell functions, and aberrations of protein glycosylation are associated with various malignancies including cancer. In this chapter, we provide a detailed protocol for MALDI MS analysis of permethylated N-glycans extracted from human serum proteins. The protocol includes procedures for N-glycan purification and in-solution permethylation, structural elucidation of permethylated N-glycans by MALDI-QIT-TOF MS, and construction of indices to quantify levels of certain types of glycosylation, such as fucosylation, which may serve as a potential disease biomarker.
View Article and Find Full Text PDFAssignment of glycosylation sites and site microheterogeneity is of both biological and clinical significance. Herein, the detailed N-glycosylation pattern of human serum alpha-2-macroglobulin was studied using an integrative approach, including permethylation of N-glycans, collision induced dissociation (CID) and electron transfer dissociation (ETD) of chymotryptic N-glycopeptides, and partial deglycosylation of chymotryptic N-glycopeptides with endo-β-N-acetylglucosaminidase F3 (Endo F3). Three N-glycosylation sites were found to be occupied by four biantennary complex type N-glycans using N-glycan analysis and the ETD/CID method.
View Article and Find Full Text PDFA mass spectrometric method was developed to elucidate the N-glycan structures of serum glycoproteins and utilize fucosylated glycans as potential markers for pancreatic cancer. This assay was applied to haptoglobin in human serum where N-glycans derived from the serum of 16 pancreatic cancer patients were compared with those from 15 individuals with benign conditions (5 normals, 5 chronic pancreatitis, and 5 type II diabetes). This assay used only 10 μL of serum where haptoglobin was extracted using a monoclonal antibody and quantitative permethylation was performed on desialylated N-glycans followed by MALDI-QIT-TOF MS analysis.
View Article and Find Full Text PDFThe purpose of this study was to investigate the serum metabolic difference between hepatocellular carcinoma (HCC, n = 20) male patients and normal male subjects (n = 20). Serum metabolome was detected through chemical derivatization followed by gas chromatography/mass spectrometry (GC/MS). The acquired GC/MS data was analyzed by stepwise discriminant analysis (SDA) and support vector machine (SVM).
View Article and Find Full Text PDFIn this study, very easily prepared trypsin-immobilized magnetic microspheres were applied in microwave-assisted protein digestion and firstly applied for proteome analysis by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Magnetic microspheres with small size were synthesized and modified by 3-glycidoxypropyltrimethoxysilane (GLYMO). Trypsin was immobilized onto magnetic microspheres through only a one-step reaction of its amine group with GLYMO.
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