Polypeptide with anti-bacterial function and preparation method and application thereof

A technology with multiple functions and antibacterial drugs, applied in the antibacterial field, can solve the problems of large molecular weight of natural antibacterial peptides, high purification or production costs, and easy interference of long-chain polypeptides, and achieve small molecular weight peptides, reduce bacterial drug resistance, and structure Stable and Simple Effects

Active Publication Date: 2015-07-15
SICHUAN UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0007] However, the short board of natural antimicrobial peptides is that the molecular weight is large, the purification or production cost is high, and the long-chain peptides are easily disturbed in the process of drug metabolism in the body, which is limited in clinical application.

Method used

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  • Polypeptide with anti-bacterial function and preparation method and application thereof
  • Polypeptide with anti-bacterial function and preparation method and application thereof
  • Polypeptide with anti-bacterial function and preparation method and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0034] 1. Select Fmoc-His (Trt)-Wang Resin as the resin (carrier);

[0035] 2. Fully swell the resin with DCM;

[0036] 3. Use an appropriate concentration of DBLK (hexahydropyridine + DMF) to remove the Fmoc-protecting group;

[0037] 4. Wash several times with DMF to remove DBLK;

[0038] 5. Weigh the appropriate condensing agent and activator (HBTU, NMM) and the second Fmoc-protected amino acid (Fomc-Leu-OH) at the C-terminal for coupling;

[0039] 6. The ninhydrin detection method is used for detection to ensure that the connection is relatively complete;

[0040] 7. Wash several times with DMF to wash away the remaining residues and activator condensation agent;

[0041] 8. Carry out coupling according to the amino acid sequence of SEQ ID NO.1, the method refers to steps 3-7;

[0042] 9. After connecting all the amino acids, use steps 3 and 4 to remove the final Fmoc-protecting group;

[0043] 10. Cleavage with TFA cutting solution to remove resin and amino acid prot...

Embodiment 2

[0049] Circular dichroism analysis of embodiment 3 polypeptide

[0050] Circular dichroism (CD) spectroscopy is a fast, simple and accurate method to study protein conformation in dilute solution. This experiment is used to measure the structure of the polypeptide to verify the validity of its design principle. According to literature review, circular dichroism analysis shows that the α-helical structure has a positive band near the ultraviolet wavelength of 192nm, and two negative characteristic shoulder bands at 222 and 208nm. The appearance of the α-helical structure can be confirmed by observing the circular dichroism spectral bands.

Embodiment 3

[0051] laboratory apparatus

[0052] Jasco J-1500 CD Spectrometer (Japan)

[0053] Experimental procedure

[0054] Under the condition of 25°C, the light transmission length of the measurement container is 1mm, and the wavelength range of ultraviolet light is 190nm to 240nm. The GH12 samples prepared in Examples 1 and 2 were detected respectively, and each sample was scanned 10 times to obtain the average value. The sample peptide concentration is 0.2mg / ml, which are dissolved in solution A: 0.02M PBS solution; B: 0.02M PBS solution containing 25mM SDS; C: 0.02M PBS solution containing 50% TFE (v / v).

[0055] The obtained data is calculated by the formula of molar ellipticity draw a graph such as figure 1 shown.

[0056] It can be seen from the image curve that with the participation of surfactant (SDS) and common chemical solvents (TFE), the peptide spectrum presents a typical α-helix structure, indicating that the secondary structure of the polypeptide in solution is ...

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Abstract

The invention discloses polypeptide and a preparation method and application thereof with an anti-bacterial function and belongs to the technical field of anti-bacteria. The antibacterial polypeptide comprises amino acid sequences as shown in the SEQ ID NO.1 and salt or ester thereof. The antibacterial polypeptide forms an alpha spiral structure through the specific array of specific kinds of amino acid, the spiral structure makes contact with and acts on a bacterial cell wall to cause the piercing of the cell wall, the bacterium dies, and therefore the antibacterial effect is achieved. The antibacterial polypeptide is convenient to composite, low in cost, good in effect and safe and reliable. Meanwhile, protein antibacterial agents can effectively reduce the occurrence of bacterial drug resistance, and huge potential is achieved in the direction of replacing antibiotics to be the main stream antibacterial medicine.

Description

technical field [0001] The invention relates to an antibacterial technology, in particular to an antibacterial functional polypeptide and its preparation method and application. technical background [0002] Caries is an infectious disease and the most common oral disease in humans. Untreated caries progresses to endodontic and periapical disease. Due to the high incidence and wide prevalence of dental caries, which seriously affects oral and general health, the World Health Organization has listed it as one of the three major non-communicable diseases that human beings should prevent and treat, second only to cardiovascular diseases and tumors. [0003] Caries is a multifactorial disease of dental hard tissues. The four factors, microorganisms, diet, host and time, interact to cause caries to occur. A large number of evidences have shown that the presence of bacteria is a prerequisite for caries to occur. Common pathogenic bacteria in the oral cavity include Streptococcus...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K7/08C07K1/06C07K1/04A61K38/10A61P31/04
CPCY02P20/55
Inventor 张凌琳范莹莹涂欢芯周学东李伟李继遥
Owner SICHUAN UNIV
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