Improved porcine VIP (vasoactive Intestinal peptide) and method for expressing porcine VIP in escherichia coli
A technology of Escherichia coli and expression vector, which is applied in the field of porcine VIP improved peptide and its expression in Escherichia coli, can solve the problems of complex production process, insufficient antibacterial activity, and low antibacterial spectrum, and achieve broad antibacterial spectrum, antibacterial The effect of strong bacterial ability and simple production process
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Embodiment 1
[0073] Antibacterial activity detection and safety evaluation method of porcine VIP improved peptide:
[0074] Natural animal-derived antimicrobial peptide is a kind of neuroimmunomodulatory peptide, which has a simple and clear structure, has a variety of biological activities, and has a small concentration, and has potential for development; however, its antibacterial activity is relatively low. In view of this, through molecular improvement, it aims to While improving its antibacterial activity, ensure its non-toxic side effects and strong stability.
[0075] Firstly, through the minimum inhibitory concentration experiment, porcine VIP and its improved peptide pVIP were detected m Antibacterial activity against Escherichia coli ATCC25922, Staphylococcus aureus ATCC25923 and Escherichia coli K88, based on which different concentrations of VIP and pVIP were detected m The hemolytic activity of red blood cells in SD rats and the effect on the proliferation of 3T3-L1 preadipoc...
Embodiment 2
[0077] The preparation method of porcine VIP improved peptide:
[0078] (1) Synthesis of pig VIP improved peptide gene:
[0079] The screened porcine VIP improved peptide is prepared by genetic engineering to improve its applicability.
[0080] According to the amino acid sequence, structural characteristics and physical and chemical properties of porcine VIP in GeneBank, as well as the structural basis of the antibacterial peptide exerting antibacterial activity, it was improved. Amino acid sequences before and after improvement are as follows:
[0081] Before improvement: HSDAVFTDNYTRLRKQMAVKKYLNSILN,
[0082] Improved: FTANYTRLRRQLAVRRYLAAILRRR,
[0083] In order to avoid the toxicity of the pig VIP improved peptide of the present invention to E. coli host bacteria, TrxA was fused with the improved antibacterial peptide VIP, and a stop codon TAA was added to the nucleotide sequence of the antimicrobial peptide VIP analogous peptide, and the 5' end The enterokinase recog...
Embodiment 3
[0100] Detection of antibacterial activity of recombinantly expressed porcine VIP improved peptide:
[0101] Detection of Antibacterial Activity of Recombinantly Expressed Porcine VIP Modified Peptide Using Oxford Cup Method, Escherichia coli ATCC 25922 and Staphylococcus aureus ATCC 25923 to OD 600 About 0.5, prepare 100mL of MHB medium containing 1.5% agar, cool the sterilized MH medium to about 50°C, add 1mL of the above bacterial solution, mix well and pour the plate. After the medium solidified, place an Oxford cup vertically on the surface of the medium, add the sample to be tested into the Oxford cup, and incubate at 37°C for 24 hours. Observe the size of the inhibition zone, the higher the antibacterial activity and concentration of the sample, the larger the inhibition zone. The test results are shown in Figure 5, which shows that the pig VIP improved peptide prepared by the method of recombinant expression in Escherichia coli used in the present invention has strong...
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