Production and characterization of recombinant human beta‐defensin DEFB120 |
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| Authors: | Haiyan Liu Heguo Yu Aijie Xin Huijuan Shi Yihua Gu Yonglian Zhang Hua Diao Donghai Lin |
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| Institution: | 1. The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation, Key Laboratory for Chemical Biology of Fujian Province, College of Chemistry and Chemical Engineering, Xiamen University, , Xiamen, 361005 China;2. School of Life Science and Technology, China Pharmaceutical University, , Nanjing, 210009 China;3. NPFPC Key Laboratory of Contraceptives and Devices, Shanghai Institute of Planned Parenthood Research, , Shanghai, 200032 China;4. Shanghai Key Laboratory for Molecular Andrology, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, , Shanghai, 200031 China |
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| Abstract: | Public health of human beings is threatened by superbugs. Novel human beta‐defensins, which contribute to host defense against pathogen invasion and innate immune protection, might be a potent natural candidate pool for new antibiotic lead screening. In the present work, we successfully expressed and purified a novel human beta‐defensin, DEFB120, using the IMPACT‐TWIN system in Escherichia coli and identified the purified homogeneous proteins using MALDI‐TOF mass spectrometry. Then, we performed the fundamental studies on the structure and biological functions for the DEFB120 peptide. The recombinant DEFB120 peptide showed wide antimicrobial effects against E. coli, Staphylococcus aureus and Candida albicans strains without significant hemolytic activity. Furthermore, the high lipopolysaccharide (LPS)‐binding affinity in vitro indicated that DEFB120 might be associated with the inhibition of LPS‐induced inflammatory response. These results may pave a way for exploiting the essential physiological functions of DEFB120 and also for the development of natural antibiotic pools. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd. |
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| Keywords: | human beta‐defensin 120 recombinant expression antimicrobial activity LPS hemolytic activity |
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