Solid-phase synthesis method of beta-amyloid peptide 1-42

Abstract

The invention provides a solid-phase synthesis method of beta-amyloid peptide 1-42, and mainly solves the technical problems of complicated process, high cost and low yield of conventional synthesis methods. The synthesis method particularly comprises the following steps: (1) Fmoc-Ala-HMP-TentaGel resin is subjected to solid-phase synthesis; (2) the Fmoc-Ala-HMP-TentaGel resin is coupled with amino acids or Hmb (Dmb) amino acids according to a peptide sequence of the beta-amyloid peptide 1-42 to obtain beta-amyloid peptide 1-42 resin peptide; and (3) the crude beta-amyloid peptide 1-42 is obtained by cracking of the beta-amyloid peptide 1-42 polypeptide resin. The process method for preparing the beta-amyloid peptide 1-42 has the advantages of simple operation, high crude peptide purity and high comprehensive yield, and has considerable economic and practical value and wide application prospect.

Description

technical field [0001] The invention relates to the field of polypeptide solid-phase synthesis, in particular to a solid-phase synthesis method of beta amyloid peptide 1-42. Background technique [0002] β-amyloid peptide 1-42, English name is β-Amyloid(1-42), molecular formula: C 203 h 311 N 55 o 60 S 1 , molecular weight: 4514.10, its peptide sequence is: NH 2 -Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly -Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala-COOH. [0003] Alzheimer's disease (AD) is a degenerative disease of the central nervous system with a high incidence and great harm. The main clinical symptom is progressive decline in intelligence. The characteristic pathological changes are senile plaques and neurofibrillary tangles. , the number of neurons mainly decreased in the hippocampus and cortical regions. It often occurs in the elderly population. With the increasing aging of the ...

AI Technical Summary

Problems solved by technology

[0005] At present, there are two conventional preparation methods of β-amyloid peptide 1-42, biological method and chemical method. The biological method is prepared by gene protein expression. CN200810025285 discloses a method for preparing β-amyloid peptide 1-42. The process is complicated, there are many variable factors, and the cost is expensive, which is not conducive to the later industrialization

However, due to the extreme hydrophobicity of the 29-42 amino acids in the sequence, the conventional chemical synthesis method is easy to form a β-sheet conformation, which will cause the amino group to be wrapped in the folded peptide sequence and not easily exposed, increasing the difficulty of coupling subsequent amino acids. At the same time, the sensitivity of ninhydrin detection is also reduced, which may easily cause false negatives.

Lead to incomplete coupling, the generation of default peptide impurities, increase the difficulty of subsequent purification, and reduce the yield

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