Fusion protein containing fluorescent protein fragment and application of fusion protein

Abstract

The invention relates to fusion protein containing a fluorescent protein fragment and an application of the fusion protein. Specifically, the invention provides the fusion protein, and the fusion protein has a structure as shown in (P1-L1)s-A1-(X)n-A2-(L2-P2)t. (X)n or A1-(X)n in the fusion protein can promote the folding and expression of fusion target peptide, improve the solubility of the fusion protein and reduce the intermolecular interaction of the fusion protein, so that the fusion target peptide can be folded under the high concentration with commercial significance. (X)n or A1-(X)n inthe fusion protein can be digested into a plurality of oligopeptides of which the lengths are far less than the length of the target peptide, so that the separation of the oligopeptides from the target peptide is better facilitated, and the purification of the target peptide is more convenient.

Description

technical field [0001] The invention relates to the field of biotechnology, in particular to fusion proteins containing fluorescent protein fragments and uses thereof. Background technique [0002] Peptides are a class of biomolecules that are widely used in many fields of biomedical research as reagents, as therapeutic drugs in the treatment of diseases, as diagnostic agents in the detection of pathogenic bacteria, and as biomarkers. There are usually two ways to synthesize peptides, one is chemical synthesis, and the other is recombinant expression. Chemical synthesis has been used to prepare a variety of therapeutic peptides, including cortirelin, parathyroid hormone (PTH), glucagon-like peptide (GLP-1) and its derivatives exenatide and liraglu peptide, enfuvirtide, calcitonin, bivalirudin, ziconotide, sermorelin, somatorelin, secretin, teduglutide, and insulin. This method requires multi-step condensation of amino acid fragments to form peptides, and also requires tedi...

AI Technical Summary

Problems solved by technology

However, currently available fusion protein methods for peptide expression present many technical problems, especially for the generation of peptides of less than 50 amino acid residues

For example, the fusion protein in the prior art has a large molecular weight, strong hydrophobicity, difficult to separate, low specific gravity of the target protein, low fusion ratio, stable structure, difficult to digest, and a lot of dead volume on the ion column and hydrophobic column.

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