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Dipeptide based polymer materials and application of dipeptide based polymer materials in saccharide separation and glycopeptide enrichment

A technology of polymer materials and peptide compounds, applied in the field of material chemistry, can solve the problems of sugar chain biological information loss, low glycosylation coverage, and damage to sugar chain structure, achieving high repeatability, high selectivity, and improved The effect of identification number

Inactive Publication Date: 2016-01-20
WUHAN UNIV OF TECH +1
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  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

For example, there is a problem of low glycosylation coverage in lectin affinity chromatography [Kubota, et al. Loss of information [Zhang, H.; etal.Nat.Biotechnol.2003]; Hydrophilic interaction chromatography is universal for glycopeptides, but the selectivity is very low, and comprehensive glycoproteomic identification of complex biological samples cannot be achieved

Method used

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  • Dipeptide based polymer materials and application of dipeptide based polymer materials in saccharide separation and glycopeptide enrichment
  • Dipeptide based polymer materials and application of dipeptide based polymer materials in saccharide separation and glycopeptide enrichment
  • Dipeptide based polymer materials and application of dipeptide based polymer materials in saccharide separation and glycopeptide enrichment

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Experimental program
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Embodiment 1

[0050] This embodiment provides dipeptide compounds, which are screened by the following methods:

[0051] The first step: determine the binding ability between 54 dipeptide sequences with different combinations and 7 representative monosaccharides, and obtain 54 sets of measured values ​​of binding constants Ka', the number of measured values ​​of binding constants in each set is 7, Subtract the minimum value of the binding constant measurement value among the 7 binding constant measurement values ​​of each group, and then use the difference between the maximum value and the minimum value as the difference between the 7 numerical values ​​obtained after subtracting the minimum value respectively. Normalize to obtain S1' to S7' respectively, arrange S1' to S7' from small to large, and obtain the distribution of measured values ​​of binding constants, please refer to figure 1 .

[0052] In this example, N is selected as 54, which is mainly selected according to the hydrophilic...

Embodiment 2

[0081] Preparation of acrylamidated dipeptide functional monomer (taking Pro-Asp, Pro-Glu, Tyr-Asp as examples):

[0082] Under ice bath conditions, 1.15g (5mmol) Pro-Asp and 1.01g (5mmol) triethylamine were dissolved in 30mL of anhydrous chloroform / DMF (volume ratio: 1:1) mixed solution, and under stirring conditions, 0.453 g (5 mmol) of acryloyl chloride was added dropwise to the above solution, and after the dropwise addition, the reaction was continued for 6 hours at room temperature. After the reaction was completed, the reaction liquid was extracted four times with 30 mL of pure water, the aqueous phase solutions were combined, most of the water was distilled off under reduced pressure, and then lyophilized. The crude product was separated and purified by liquid chromatography, and a C18 reverse-phase semi-preparative column was used for separation in reverse-phase mode. Finally, 0.92 g of white powder was obtained with a yield of 65%. The structure of the product was ...

Embodiment 3

[0090] Grafting method of dipeptide polymer on planar substrate:

[0091] Taking the polymerized Pro-Asp as an example, add 1.0g of acrylamidated Pro-Asp to a 25mL flask, and add 3mL of H at the same time 2 O, 3mLCH 3 OH and 3mL DMF were used as solvents; nitrogen gas was introduced under stirring, and after the monomers were fully dissolved, 0.032g of catalyst CuBr and 0.16mL of PMDETA or bipyridine ligand were added under the protection of nitrogen, and then the reaction system was evacuated—nitrogen gas was filled to remove the reaction The residual oxygen in the system; the brominated Si, SiO 2、 Au, Ag, Pt, CuO, Al 2 o 3 、TiO 2 , ZrO 2 or Fe 3 o 4 The surface is immersed in the prepared reaction solution; the temperature of the flask is controlled at 60°C and left to react for 4-6 hours; after the reaction is completed, use DMF, H 2 O washed the polymer grafted surface sequentially to obtain the surface modified by Pro-Asp dipeptide polymer material, the thickness ...

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Abstract

The invention relates to a screening method of dipeptide functional monomers having excellent separating capacity on saccharide. A dipeptide compound obtained on the basis of screening of standard deviation parameter D and R values is constructed, the dipeptide compound obtained through screening is further coupled with a group containing double bonds, polymerizable dipeptide functional monomers are obtained and are polymerized on surfaces of various matrixes, and a series of polymer modified chromatographic stationary phase materials are obtained. The materials have excellent separating capacity on oligomeric galactose, oligomeric fructose and sialic acid derivatives; meanwhile, the materials have excellent selective enrichment performance on the glycopeptide and separating capacity on a carbohydrate chain structure, have very high glycopeptide recovery rate and repeatability and have the wide application prospect in the fields of posttranslational modification proteomics research and the like.

Description

technical field [0001] The invention belongs to the field of material chemistry, in particular to a dipeptide-based polymer material and its application in sugar separation and glycopeptide enrichment. Background technique [0002] Glycosylation of proteins regulates many important biological processes in eukaryotic cells, including immune response, cell adhesion and migration. Variations in protein glycosylation are associated with the occurrence of many diseases. In addition, the vast majority of existing tumor markers and protein drugs are glycoproteins. Therefore, it is very important to characterize the structure of glycoproteins. However, the concentration of glycopeptides in biological samples is very low (the first 22 proteins in the high-abundance proteins in the human body account for about 99% of the total plasma proteins, and the content of glycoproteins is roughly one-thousandth). Ion suppression by glycopeptides, especially albumin and immunoglobulins, makes...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K5/078C07K5/065C07K5/072C08F120/60C07K1/14
Inventor 孙涛垒梁鑫淼卿光焱李秀玲
Owner WUHAN UNIV OF TECH
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