Effect of N- and C-Terminal Modifications on Cytotoxic Properties of Antimicrobial Peptide Tachyplesin I

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 modifi...

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Bibliographic Details
Published in:Bulletin of experimental biology and medicine 2017-04, Vol.162 (6), p.754-757
Main Authors: Kuzmin, D. V., Emelianova, A. A., Kalashnikova, M. B., Panteleev, P. V., Ovchinnikova, T. V.
Format: Article
Language:English
Subjects:
A549 Cells
Acetylation
Amides - chemistry
Amino Acid Sequence
Antimicrobial agents
Antimicrobial Cationic Peptides - chemical synthesis
Antimicrobial Cationic Peptides - toxicity
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cell Survival - drug effects
Cells (Biology)
Cytotoxicity
Cytotoxins - chemical synthesis
Cytotoxins - toxicity
DNA-Binding Proteins - chemical synthesis
DNA-Binding Proteins - toxicity
Erythrocytes - drug effects
Escherichia coli - genetics
Escherichia coli - metabolism
Gene Expression
HEK293 Cells
HeLa Cells
Hemolysis - drug effects
Humans
Inhibitory Concentration 50
Internal Medicine
Laboratory Medicine
Pathology
Peptides
Peptides, Cyclic - chemical synthesis
Peptides, Cyclic - toxicity
Protein Stability
Proteolysis
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Recombinant Proteins - toxicity
Solid-Phase Synthesis Techniques - methods
Structure-Activity Relationship
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Description
Summary: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.
ISSN:0007-4888
1573-8221
DOI:10.1007/s10517-017-3705-2