Novel antibacterial active peptide based on human autocrine

A technology of antibacterial activity and active peptide, which is applied in the field of biochemistry, can solve the problems of consuming a lot of manpower, material resources, large amount of calculation, and insufficient structural diversity, and achieve the effects of low cost, high biological stability, and avoiding immune damage

Active Publication Date: 2015-04-08
THE SECOND XIANGYA HOSPITAL OF CENT SOUTH UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, these methods are all based on the structure of natural antimicrobial peptides. Although they can improve some of their defects, the designed molecules have the problem of insufficient structural diversity; although the combined peptide library method can well meet the requirements of molecular diversity, and can Realize the high-throughput screening of antimicrobial peptides, but the experiment requires a lot of m

Method used

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  • Novel antibacterial active peptide based on human autocrine
  • Novel antibacterial active peptide based on human autocrine
  • Novel antibacterial active peptide based on human autocrine

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0037] The 70-101 AA sequence segment of SPLUNC1 protein was selected as the core region of the active peptide to prepare a new type of antibacterial active peptide AMP1 (NLPLLDILKPGGGTSGGLLGGLLGKVTSVIPG).

[0038] (1) Activated resin: wash and activate Wang's resin with dichloromethane (DCM), stand-by;

[0039] (2) Cross-linking of Fmoc-protected amino acids and resins: Dimethylformamide (DMF), DIEA (N,N-diisopropylethylamine), O-benzotriazole-tetramethylurea hexafluoro Phosphate (HBTU) is mixed with the C-terminal amino acid of the Fmoc-protected target polypeptide; then the mixture is added to the activated resin, and the reaction is shaken to cross-link the Fmoc-protected amino acid with the resin;

[0040] (3) Remove the first Fmoc protecting group and expose the active amino group: use a DMF solution containing 20% ​​piperidine as a deprotecting agent, soak the Fmoc-protected polypeptide 3 fixed on the resin with the deprotecting agent Minutes, drain the resin, filter o...

Embodiment 2

[0048] The 165-191 AA sequence segment of SPLUNC1 protein was selected as the core region of the active peptide to prepare a new type of antibacterial active peptide AMP2 (AVRDKQHRIHLVLGDCTHSPGSLQISL).

[0049] The preparation method and steps of the novel antibacterial active peptide AMP2 are the same as the preparation method and steps of the novel antibacterial active peptide AMP1, refer to Example 1.

[0050] The HPLC spectrum of AMP2 is as follows image 3 As shown, the mass spectrum as Figure 4 shown. Depend on image 3 , 4 It can be seen that the purity and molecular weight of AMP2 both meet the design requirements.

Embodiment 3

[0052] The 199-234 AA sequence segment of SPLUNC1 protein was selected as the core region of the active peptide to prepare a novel antibacterial active peptide AMP3 (PIQGLLDSLTGILNKVLPHLVQGNVCPLVNHVLRGL).

[0053] The preparation method and steps of the novel antibacterial active peptide AMP3 are the same as the preparation method and steps of the novel antibacterial active peptide AMP1, refer to Example 1.

[0054] The HPLC spectrum of AMP3 is as follows Figure 5 As shown, the mass spectrum as Image 6 shown. Depend on Figure 5 , 6 It can be seen that the purity and molecular mass of AMP3 both meet the design requirements.

[0055] The physical and chemical properties of the designed and prepared new antibacterial active peptide AMP1-AMP3 and SPLUNC1 protein are shown in Table 1. The physical and chemical properties of the designed and prepared new antibacterial active peptide AMP1-AMP3 are significantly different from those of SPLUNC1 protein. The appropriate peptide c...

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Abstract

The embodiment of the invention discloses novel antibacterial active peptide based on human autocrine. According to the novel antibacterial active peptide, SPLUNC1 protein excreted by a human body is taken as a template, a combinational design of novel antibacterial peptide is carried out by combining the molecular design and synthesis theories of antibacterial peptides (AMP) with a biological evolution conserved gene principle based on antibacterial mode sequence requirements and modification on amino acid structures and residue structures of prepotent loci, and a mature peptide synthetic technique is utilized for preparing novel antibacterial active peptide; the length of each AMP is only equal to 1/10 of that of primary SPLUNC1 protein, furthermore, the synthesis is easy, and the cost is low; the new synthesized AMP is derived from highly conserved amino acid sequences of the human body and has high biological stability and a proper half-life period; in vitro experiments prove that the new synthesized AMP has relatively good water solubility and broad-spectrum antibacterial and anti-fungus actions and is expected to be developed into a new antibacterial clinical drug, and hemolysis is nearly avoided.

Description

technical field [0001] The invention belongs to the technical field of biochemistry, and in particular relates to a class of novel antibacterial active peptides secreted by the human body itself. Background technique [0002] Since the invention of antibiotics, humans have made great achievements in controlling and treating microbial infections. However, with the continuous use of antibiotics, microbial resistance has become a major problem in clinical microbial infection control, so that there is a lack of first-line drugs to inhibit or kill certain microbial bacteria. In clinical drug treatment, staphylococci and enterococci resistant to vancomycin, Gram-negative bacteria producing extended-spectrum β-lactamase, etc. have appeared, which seriously threaten human health. Therefore, the development of antibacterial drugs with novel antibacterial mechanisms is an important way to solve antibiotic resistance. [0003] Antimicrobial peptides (AMP) refer to small molecule basi...

Claims

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Application Information

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IPC IPC(8): C07K14/47A61P31/10A61P31/04
CPCC07K14/47
Inventor 卜艳红莫喜明周后德
Owner THE SECOND XIANGYA HOSPITAL OF CENT SOUTH UNIV
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