Recombinant expression and biological characterization of the antimicrobial peptide fowlicidin-2 in Pichia pastoris.

Autor: LI-WEI XING, SHI-XUN TIAN, WEI GAO, NA YANG, PEI QU, DI LIU, JIAN JIAO, JUE WANG, XING-JUN FENG
Předmět:
Zdroj: Experimental & Therapeutic Medicine; Oct2016, Vol. 12 Issue 4, p2324-2330, 7p
Abstrakt: Fowlicidins are a group of cathelicidin antimicrobial peptides that were initially identified in chickens. Fowlicidin-2, which is composed of 31 amino acids, is widely expressed in the majority of tissues in chickens and has an important role in innate immunity. In the present study, a recombinant expression system for fowlicidin-2 was successfully constructed using Pichia pastoris X-33 and the expression vector pPICZα-A. Under the optimized fermentation conditions, 85.6 mg fowlicidin-2 with >95% purity was obtained from 1 liter culture medium following purification by ion exchange chromatography and reversed phase high performance liquid chromatography. The recombinant fowlicidin-2 exhibited broad spectrum antimicrobial activity and had a minimum inhibitory concentration ranging from 1 to 4 μM. Furthermore, recombinant fowlicidin-2 exhibited hemolytic activity, promoting 50% human erythrocyte hemolysis in the concentration range of 128-256 μM, and anticancer activity, resulting in the death of 50% of A375 human malignant melanoma cells in the concentration range of 2-4 μM. The results of the present study suggest that recombinant fowlicidin-2 may be a promising candidate for therapeutic applications. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index