Antibacterial oligopeptide LBD-S and application and medicine thereof

A LBD-S, short peptide technology, applied in the direction of antibacterial drugs, peptides, depsipeptides, etc., can solve the problems of eukaryotic cytotoxicity and the unsatisfactory activity of natural antibacterial peptides, and achieve high antibacterial activity, low hydrophobicity, Hydrophilic and lipophilic effect

Active Publication Date: 2021-10-29
北京师范大学珠海校区
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0003] Since the activities of many natural antimicrobial peptides identified and isolated are not ideal, or have certain toxicity to eukaryotic cells, the design and modification of antimicrobial peptides has become the preferred method to overcome such shortcomings, which will help future development to be attractive. novel antimicrobial peptide

Method used

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  • Antibacterial oligopeptide LBD-S and application and medicine thereof
  • Antibacterial oligopeptide LBD-S and application and medicine thereof
  • Antibacterial oligopeptide LBD-S and application and medicine thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0046] Example 1 Transformation of antimicrobial peptide LBD short peptide based on MjALF-D

[0047]According to the analysis of the physical and chemical properties and structural information of the LBD short peptide of MjALF-D, the analysis software uses the ProtParam online analysis software (http: / / www.expasy.org / tools / protparam) in the Expert Protein Analysis Software (ExPASy) website And The Antimicrobial Peptide Database (APD, http: / / aps.unmc.edu / AP / main.php) online analysis software to obtain relevant parameters of the peptide. The analysis of the arrangement of hydrophilic and hydrophobic amino acids of short peptides and the helical wheel projection were performed using the online analysis software Heliquest analysis (http: / / heliquest.ipmc.cnrs.fr / cgi-bin / ComputParams.py) (Gautier et al., 2008 )conduct. Sequence alignment of the LBD short peptide (LBD-ALF) of MjALF-D in the APD antimicrobial peptide system, and amino acid substitutions were carried out according to ...

Embodiment 2

[0054] The artificial synthesis of embodiment 2 antibacterial short peptide LBD-S short peptide

[0055] The antibacterial LBD short peptide that has been modified and designed is synthesized. The synthesis method is based on solid-phase chemical synthesis. The synthesis direction is from the C-terminal to the N-terminal of the LBD-S short peptide, and the N-terminal is acetylated, and the C-terminal is amidated to enhance the stability of the synthetic peptide. Sexuality. The carboxy-terminus and amino-terminus of LBD-S are cysteine, forming a disulfide bond. The synthesized LBD-S short peptide was purified by reverse-phase high-performance liquid chromatography and its purity was tested. The results are as follows: figure 2 shown.

[0056] from figure 2 It can be seen from the figure that the synthesized antibacterial short peptide LBD-S has only one prominent peak, and the purity is high (95.0749%).

Embodiment 3

[0057] The MIC of embodiment 3 antimicrobial short peptide LBD-S and MBC measure

[0058] The detection and analysis of protein minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) is carried out by liquid growth inhibition assay, and the specific determination method refers to the following literature:

[0059] [1] Ying P, Libing Z, Mao Y, et al.The antibacterial activity and mechanism analysis of piscidin 5 like from Larimichthys crocea[J].2019,92:43-49.

[0060] The results are shown in Table 2.

[0061] Table 2 MIC and MBC of LBD-ALF and modified LBD-S short peptide (unit: μM)

[0062]

[0063]

[0064] Note: NT: not detected.

[0065] As can be seen from Table 2, the modified antibacterial short peptide LBD-S is effective against Gram-positive bacteria (including Bacillus subtilis, Corynebacterium glutamicum, Micrococcus lyticus and Micrococcus luteus) and Gram-positive bacteria. Negative bacteria (including Photobacterium mermaidus...

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Abstract

The invention provides an antibacterial oligopeptide LBD-S as well as application and a medicine thereof, and relates to the field of biotechnology. The invention provides an antibacterial oligopeptide LBD-S. The amino acid sequence of the antibacterial oligopeptide LBD-S is CTKKVKPDLKRFEKYFKGTVTC. The inventor finds that the antibacterial oligopeptide LBD-S has low hydrophobicity, high hydrophilicity and lipophilicity and high antibacterial activity, and the antibacterial oligopeptide LBD-S can be applied to gram-negative bacteria and gram-positive bacteria, such as bacillus subtilis, corynebacterium glutamicum, micrococcus lyticus, micrococcus luteus, photobacterium damsonii and the like. Compared with the antibacterial oligopeptide LBD-ALF before modification, the antibacterial oligopeptide LBD-S provided by the invention has the advantages that the inhibition effect on the bacillus subtilis, the corynebacterium glutamicum and the micrococcus lyticus is obviously enhanced, and the antibacterial oligopeptide LBD-Scan be used for preparing antibacterial products.

Description

technical field [0001] The invention relates to the field of biotechnology, in particular to an antibacterial short peptide LBD-S and its application and medicine. Background technique [0002] The problem of biological antibiotic resistance is one of the main problems affecting public health and clinical practice. Antimicrobial peptides (AMPs), as an important alternative to antibiotics, have attracted great attention. Most of the research work involves Identification of antimicrobial peptides, in vitro activity and mode of action, and mechanisms of microbial resistance. The lipopolysaccharide-binding domain (LBD) of anti-lipopolysaccharide factors (ALFs) is the main functional element of ALF and has antibacterial activity. It generally has 22 amino acid residues and a disulfide bond structure composed of two cysteines. Moreover, the LBD is considered a functional domain for antimicrobial and antiviral activities. [0003] Since the activities of many natural antimicrobia...

Claims

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Application Information

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IPC IPC(8): C07K14/00A61K38/16A61P31/04
CPCC07K14/00A61P31/04A61K38/00
Inventor 张鹤千余祥勇毛勇
Owner 北京师范大学珠海校区
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