N-phosphorylated peptide enrichment method

A phosphorylated peptide, phosphorylation technology, applied in the preparation method of peptide, chemical instrument and method, peptide and other directions
CN106478768APending Publication Date: 2017-03-08DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI

Patent Information

Authority / Receiving Office
CN · China
Current Assignee / Owner
DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
Publication Date
2017-03-08

Smart Images

  • Figure 1
    Figure 1
  • Figure 2
    Figure 2
  • Figure 3
    Figure 3
Patent Text Reader

Abstract

The present invention relates to an N-phosphorylated peptide enrichment method. According to the method, O-phosphorylated peptide interference in a peptide sample is removed through beta-elimination, and the N-phosphorylated modified peptide in the sample is enriched by using a magnetic mesoporous titania composite nanometer material; the O-phosphorylated modification on serine and threonine is removed through a beta-elimination method under an alkaline condition so as to form stable dehydroalanine and beta-methyl dehydroalanine; a magnetic Fe3O4 nanometer material is synthesized through a solvent method, titanium dioxide is wrapped on the surface through a sol-gel method, and hole amplification is performed through a hydrothermal method to obtain the magnetic mesoporous titania composite nanometer material; and the magnetic mesoporous titania composite nanometer material can specifically enrich the N-phosphorylated peptide under a weak acid buffer system. According to the present invention, the beta-elimination and specific enrichment combined method is used for enriching the N-phosphorylated peptide in the sample.
Need to check novelty before this filing date? Find Prior Art

Description

technical field

[0001] The invention relates to a method for specifically enriching N-phosphorylated peptides in combination with a magnetic mesoporous titanium dioxide nanocomposite material after β-elimination to remove O-phosphorylated peptides of serine and threonine. Background technique

[0002] Protein phosphorylation modification is involved in almost all life activities such as cell proliferation and apoptosis, development and differentiation, signal transduction (Nat. Biotechnol, 2005, 23, 94-101). In particular, the N-phosphorylation modification of proteins plays a pivotal role in core life processes such as life evolution, nucleosome assembly, cell transcription, and signal transduction. Therefore, it is of great biological significance to study the phosphorylation modification of proteins. Among them, the phosphorylation modification (O-phosphorylation modification) on the hydroxyl group of serine, threonine and tyrosine, its P-O phosphate bond has good stabil...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More