Study on biological activity and stability of new derivative KW-WK from bovine lactoferricin

Abstract

Abstract: This study had designed the new antimicrobial peptide KWRRWQWRRWK-NH2 (KW-WK) with the fragment of bovine lactoferricin--LFcinB18-28 as its parent peptide, on the basis of its high charge and strong hydrophobicity, and according to the design idea of symmetrical structure to introduce the amino acids R and W to replacement. The secondary structure, antibacterial activity, hemolysis activity, cell toxicity and stability of the KW-WK were determined by circular dichroism spectroscopy, broth micro-dilution and MTT method. The results showed that KW-WK was a nonregular curl in aqueous solution, however, it was a α-helix structure in the simulation environment of cell membrane. The minimal inhibitory concentration (MIC) of KW-WK ranged from 4 to 128μmol/L, so the bacteriostatic activity of KW-WK was strong. The hemolytic rate was less than 5% when the concentration of KW-WK was 256μmol/L, this showed that the hemolytic rate of it was low. The therapy index of KW-WK was 9.14, and the cytotoxicity was relatively low, thus the cell selectivity was relatively high. In addition, with the heating treatment 100 ℃ for 1 h, KW-WK still possessed rather a high antibacterial activity. However, the enzyme stability of KW-WK has greatly improved than LFcinB18-28. Therefore, the new antimicrobial peptide KW-WK has showed a great application potential in the fields of food, medicine, livestock and etc.

Key words: KW-WK peptide, antibacterial activity, hemolytic activity, cytotoxicity, stability

CLC Number:

Q511

Jun-Cai HOU Dongfei LI Jia-Yin LU. Study on biological activity and stability of new derivative KW-WK from bovine lactoferricin[J]. FOOD SCIENCE, 0, (): 0-0.

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