Abstract
Antibacterial peptides have received increasing attention as a new pharmaceutical substance. But the molecular mechanism of lysis is still poorly understood. CMIV gene and mutant CMIV gene in GST fusion system were expressed. After cleaving with different cleavage reagents, the peptide with an excess of N-terminus and with an un-amidated C-terminus stopped the activity while the peptide with an excess Asn at the C-terminus had the activity level the same as natural CMIV. The results showed that the terminal structure of cecropin CMIV played an important role in its biological activity.
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Project supported by the Jiangsu Province Applied Research Project.
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Dou, F., **e, W., Dong, X. et al. The terminal structure plays an important role in the biological activity of cecropin CMIV. Sci. China Ser. C.-Life Sci. 42, 494–500 (1999). https://doi.org/10.1007/BF02881773
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DOI: https://doi.org/10.1007/BF02881773