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Polyethylene glycol-modified human interferon and human antibacterial peptide fusion protein

A fusion protein and polyethylene glycol technology, applied in the field of bioengineering, can solve problems such as small molecular weight

Inactive Publication Date: 2016-02-17
GUANGDONG ZIJIN ZHENGTIAN PHARMA
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

The main problem of interferon in clinical use is that due to its small molecular weight, it is easily degraded by proteases in serum and filtered out by glomeruli.

Method used

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  • Polyethylene glycol-modified human interferon and human antibacterial peptide fusion protein
  • Polyethylene glycol-modified human interferon and human antibacterial peptide fusion protein
  • Polyethylene glycol-modified human interferon and human antibacterial peptide fusion protein

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Embodiment Construction

[0035] The present invention will be further described below in conjunction with the accompanying drawings and implementation examples, but the present invention is not limited thereto.

[0036] Apparent molecular weight of 1PEG

[0037] The SDS-PAGE results of PEG with three molecular weights are shown in figure 1 .

[0038] Compared with protein markers, PEG 5000 The molecular weight is about 14000, PEG 10000 The molecular weight is about 29000, PEG 20000 The weight is about 40000, which is larger than the actual molecular weight. PEG 5000 with PEG 10000 About 3 times larger, PEG 20000 About 2 times larger. The reason for the large size is related to the fact that the molecular size measured by SDS-PAGE is based on the chain length as the standard. Under the condition of the same chain length, the average molecular weight of amino acids constituting the chain length unit is larger than that of ethylene glycol, so in the system with protein as the standard control, t...

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Abstract

The invention discloses polyethylene glycol-modified human interferon IFN-alpha 2 alpha and human antibacterial peptide LL-37 fusion protein. The obtained IFN-alpha 2 alpha and LL-37 fusion protein have IFN-alpha 2 alpha antiviral activity and LL-37 antibacterial activity, at the same time, half-life period of rats is prolonged from 9.3 hours for IFN-alpha 2 alpha by single usage to more than 78 hours.

Description

technical field [0001] The invention belongs to the technical field of biological engineering Background technique [0002] The Cathelicidin family is a class of conserved antimicrobial peptides expressed in mammals, birds, fish and reptiles. LL-37 is the only Cathelicidin family antimicrobial peptide synthesized by the human body, mainly expressed and synthesized by immune cells and epithelial cells. The sequence of LL-37 is LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES, named because the first two are LL (leucine) and the sequence length is 37. LL-37 combines with the hydrophilic part of the bacterial cell membrane phospholipid through the amphiphilic superhelix of positive 6 positive charges formed in the structure, and then its hydrophobic part flips and inserts into the phospholipid bilayer, thereby causing the destruction of the cell membrane. LL-37 is effective against Gram-positive and negative bacteria, and has a broad antibacterial spectrum, which has attracted extensive...

Claims

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Application Information

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IPC IPC(8): C07K19/00
Inventor 万徐萍
Owner GUANGDONG ZIJIN ZHENGTIAN PHARMA
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