We analyze the effects of N-terminal acetylation and C-terminal amidation on the cytotoxic properties of β-hairpin antimicrobial peptide tachyplesin I. MTT-assay showed that modified tachyplesin I exhibited increased cytotoxicity toward both tumor and normal human cells. Hemolytic activity of modified tachyplesin I was also higher than that of the initial molecule. In contrast to non-modified tachyplesin I, the peptide with C- and N-terminal modifications is resistant to proteolytic degradation in fresh human serum. C- and N-terminal modifications make tachyplesin I more attractive prototype of anticancer drug due to its more potent cytotoxic effect and better pharmacokinetic properties.
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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 162, No. 12, pp. 722-725, December, 2016
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Kuzmin, D.V., Emelianova, A.A., Kalashnikova, M.B. et al. Effect of N- and C-Terminal Modifications on Cytotoxic Properties of Antimicrobial Peptide Tachyplesin I. Bull Exp Biol Med 162, 754–757 (2017). https://doi.org/10.1007/s10517-017-3705-2
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DOI: https://doi.org/10.1007/s10517-017-3705-2