The invention discloses a group of low-
toxicity broad-spectrum antibacterial peptides containing a central PXXP hinge structure and application of the low-
toxicity broad-spectrum antibacterial peptides. The low-
toxicity broad-spectrum
antibacterial peptide is obtained by adopting a de novo design mode, using
lysine (Lys, K) with positive charges and hydrophobic
tryptophan (Trp, W), alternately, repeatedly and symmetrically arranging two amino acids, and introducing a PXXP hinge structure containing
proline into the symmetric center of an
antibacterial peptide sequence. The structural general formula is (KW) nPXXP (WK) n, XX = KK, n = 2-4, or XX = WK, n = 2-3. An in-vitro antibacterial experiment shows that the
antibacterial peptide disclosed by the invention has broad-spectrum
antibacterial activity; the preferred antibacterial
peptide has the advantages of low
hemolysis toxicity and
high serum stability. Induced
drug resistance experiments show that the preferred antibacterial
peptide has the characteristic of low
drug resistance generation. An in-vivo
acute toxicity experiment result shows that compared with a contrast
drug Polymyxin B, the preferable antibacterial
peptide disclosed by the invention has higher in-vivo safety. Therefore, the compound has a good application prospect in preparation of clinical antibacterial drugs, and is expected to become a novel antibiotic candidate drug.