Cyclization of antimicrobial peptide CycP-1 targeting multi-drug resistant klebsiella pneumoniae, composition and application thereof

By designing the cyclized antimicrobial peptide CycP-1 and combining it with antibiotics, the problems of strong nephrotoxicity of existing antibiotics and poor stability of antimicrobial peptides were solved, achieving highly efficient antibacterial inhibition and drug resistance reversal against multidrug-resistant Klebsiella pneumoniae, and providing a new antimicrobial strategy.

CN122036889BActive Publication Date: 2026-07-24湖北江夏实验室 +1
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Patent Information

Application Number
CN202610495860.X
Authority / Receiving Office
CN · China
Patent Type
Patents(China)
Current Assignee / Owner
Filing Date
2026-04-15
Publication Date
2026-07-24
Estimated Expiration
2046-04-15

AI Technical Summary

Technical Problem

Existing antibiotics such as polymyxin are highly nephrotoxic to Klebsiella pneumoniae and exhibit severe drug resistance. Antimicrobial peptides have poor stability in vivo and are easily hydrolyzed by proteases, which limits their application.

Method used

A cyclized antimicrobial peptide, CycP-1, with intramolecular disulfide bonds was designed. By synthesizing and oxidizing linear peptides to form intramolecular disulfide bonds, stability was improved, and it was used in combination with a variety of antibiotics to enhance antibacterial effects and reverse drug resistance.

Benefits of technology

CycP-1, an antimicrobial peptide, exhibits significant antibacterial activity against multidrug-resistant Klebsiella pneumoniae. It can be used in combination with antibiotics to enhance antibacterial effects, reverse or reduce drug resistance, and significantly slow down the development of drug resistance. In vivo experiments have shown that it has significant therapeutic effects on pan-drug-resistant bacterial infections.

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Abstract

The application belongs to the technical field of biological medicine, and discloses a cyclic antibacterial peptide CycP-1 targeting multi-drug resistant Klebsiella pneumoniae, a composition and application thereof. The amino acid sequence of the antibacterial peptide is shown in SEQ ID NO. 1, the first and the 24th cysteine residues in the molecule form a disulfide bond, and the antibacterial peptide shows a good in-vitro protease stability in a cyclic conformation. Experiments show that the antibacterial peptide has a significant inhibitory effect on multi-drug resistant and pan-drug resistant Klebsiella pneumoniae, and the antibacterial effect can be enhanced, the drug resistance can be reversed or reduced, and the generation of drug resistance can be delayed when the antibacterial peptide is combined with antibiotics. In-vivo experiments of a mouse pneumonia model further prove that after oral administration of the antibacterial peptide, the bacterial load in the lung tissue of a mouse infected with pan-drug resistant Klebsiella pneumoniae can be significantly reduced, the pathological damage in the lung can be reduced, and the survival rate of the infected mouse can be significantly improved, and the effect is better when the antibacterial peptide is combined with polymyxin B.
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