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PNGase H + variant from Rudaea cellulosilytica with improved deglycosylation efficiency for rapid analysis of eukaryotic N-glycans and hydrogen deuterium exchange mass spectrometry analysis of glycoproteins.
Rapid Commun Mass Spectrom
November 2022
Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.
The analysis of glycoproteins and the comparison of protein N-glycosylation from different eukaryotic origins require unbiased and robust analytical workflows. The structural and functional analysis of vertebrate protein N-glycosylation currently depends extensively on bacterial peptide-N4-(N-acetyl-β-glucosaminyl) asparagine amidases (PNGases), which are indispensable enzymatic tools in releasing asparagine-linked oligosaccharides (N-glycans) from glycoproteins. So far, only limited PNGase candidates are available for N-glycans analysis, and particularly the analysis of plant and invertebrate N-glycans is hampered by the lack of suitable PNGases.
View Article and Find Full Text PDFEffect of -glycosylation on horseradish peroxidase structural and dynamical properties.
Comput Struct Biotechnol J
June 2022
Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, Zagreb HR-10000, Croatia.
The effect of different branching types of glycosylation on the structure and dynamics of the horseradish peroxidase (HRP) and an engineered split horseradish peroxidase (sHRP) was studied using all-atom molecular dynamics (MD) simulations. Although tertiary structures of both proteins are stable in the presence, as well as in the absence of glycans, differences in the dynamical properties regarding the presence of glycans were noticed. Fluctuations in the protein structure along both proteins are decreased when glycosylation is introduced.
View Article and Find Full Text PDFBowl-like mesoporous polydopamine with size exclusion for highly selective recognition of endogenous glycopeptides.
Talanta
October 2021
Zhejiang Provincial Key Laboratory of Advanced Mass Spectrometry and Molecular Analysis, PR China; Institute of Mass Spectrometry, School of Materials Science & Chemical Engineering, Ningbo University, Ningbo, 315211, PR China. Electronic address:
It has been confirmed that endogenous glycopeptide plays an important role in a variety of pathological and physiological processes. However, direct analysis of endogenous glycopeptide is still a great challenge owing to the low abundance of endogenous glycopeptides and the presence of a large number of interfering substances such as large-sized proteins and heteropeptides in complex biological sample. Herein, we reported a novel bowl-like mesoporous polydopamine nanoparticle modified by carrageenan (denoted as MPDA@PEI@CA) with strong hydrophilicity and size-exclusion effect for high specificity enrichment of endogenous glycopeptides.
View Article and Find Full Text PDFA hydrophilic two-dimensional titanium-based metal-organic framework nanosheets for specific enrichment of glycopeptides.
Anal Chim Acta
July 2020
Jiangsu Key Laboratory of Biofunctional Materials, Jiangsu Collaborative Innovation Center of Biomedical Functional Materials, College of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210023, China. Electronic address:
A hydrophilic two-dimensional titanium-based metal-organic framework (MOF) nanosheets were prepared and applied to improve the glycopeptides enrichment efficiency. Seventeen N-linked glycopeptides from horseradish peroxidase (HRP) tryptic digests were readily identified and the results showed highly improved signal intensities. As the molar ratio of the mixture of tryptic digests of HRP, glycoprotein (HRP), and nonglycoprotein (BSA) reached 1:800:800, good selectivity of the Ti-MOF nanosheets were still clearly observed.
View Article and Find Full Text PDFHydrophilic maltose-modified magnetic metal-organic framework for highly efficient enrichment of N-linked glycopeptides.
J Chromatogr A
March 2020
College of Chemistry, Tianjin Key Laboratory of Biosensing and Molecular Recognition, Nankai University, Tianjin 300071, China; Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116011, China.
Biomedical sciences, and in particular disease biomarker research, demand highly selective and efficient glycoproteins/peptides enrichment platforms. In this work, a facile strategy to prepare hydrophilic maltose-functionalized magnetic metal-organic framework loaded with Au nanoparticles (denoted as magMOF@Au-maltose) for highly efficient enrichment of N-linked glycopeptides. In brief, carboxyl-functional FeO nanospheres were firstly coated with a Zr-based MOF shell, the resulting MOF was then loaded with Au nanoparticles in situ and then modified with thiol-functional maltose via Au-S bonds to obtain magMOF@Au-maltose with core-shell structure.
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