Anti-breast cancer synthetic peptides derived from the Anabastestudineus skin mucus fractions
Previous study has shown the antimicrobial activities of mucus protein extracted from Anabas testudineus . In this study, we are interested in characterizing the anticancer activity of the A. testudineus antimicrobial peptides (AMPs). The mucus was extracted, fractioned, and subjected to antibacteri...
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Published in: | Scientific reports Vol. 11; no. 1 |
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Main Authors: | , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
London
Nature Publishing Group UK
30-11-2021
Nature Publishing Group |
Subjects: | |
Online Access: | Get full text |
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Summary: | Previous study has shown the antimicrobial activities of mucus protein extracted from
Anabas
testudineus
. In this study, we are interested in characterizing the anticancer activity of the
A.
testudineus
antimicrobial peptides (AMPs). The mucus was extracted, fractioned, and subjected to antibacterial activity testing to confirm the fish's AMPs production. The cytotoxic activity of each fraction was also identified. Fraction 2 (F2), which shows toxicity against MCF7 and MDA-MB-231 were sent for peptide sequencing to identify the bioactive peptide. The two peptides were then synthetically produced and subjected to cytotoxic assay to prove their efficacy against cancer cell lines. The IC
50
for AtMP1 against MCF7 and MDA-MB-231 were 8.25 ± 0.14 μg/ml and 9.35 ± 0.25 μg/ml respectively, while for AtMP2 it is 5.89 ± 0.14 μg/ml and 6.97 ± 0.24 μg/ml respectively. AtMP1 and AtMP2 treatment for 48 h induced breast cancer cell cycle arrest and apoptosis by upregulating the p53, which lead to upregulate pro-apoptotic BAX gene and downregulate the anti-apoptotic BCL-2 gene, consequently, trigger the activation of the caspase-3. This interaction was supported by docking analysis (QuickDBD, HPEPDOCK, and ZDOCK) and immunoprecipitation. This study provided new prospects in the development of highly effective and selective cancer therapeutics based on antimicrobial peptides. |
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ISSN: | 2045-2322 |
DOI: | 10.1038/s41598-021-02007-6 |