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Mar. Drugs 2018, 16(12), 462;

Nile Tilapia Derived Antimicrobial Peptide TP4 Exerts Antineoplastic Activity Through Microtubule Disruption

Marine Research Station, Institute of Cellular and Organismic Biology, Academia Sinica, Ilan 262, Taiwan
Institute of Population Sciences, National Health Research Institutes, Zhunan 350, Taiwan
Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsinchu 300, Taiwan
The iEGG and Animal Biotechnology Center, National Chung Hsing University, Taichung 402, Taiwan
Author to whom correspondence should be addressed.
Received: 5 November 2018 / Revised: 16 November 2018 / Accepted: 16 November 2018 / Published: 22 November 2018
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Some antimicrobial peptides (AMPs) exhibit anti-cancer activity, acting on cancer cells either by causing membrane lysis or via intracellular effects. While intracellular penetration of AMPs has been shown to cause cancer cell death, the mechanisms of toxicity remain largely unknown. Here we show that a tilapia-derived AMP, Tilapia piscidin (TP) 4, penetrates intracellularly and targets the microtubule network. A pull-down assay identified α-Tubulin as a major interaction partner for TP4, and molecular docking analysis suggested that Phe1, Ile16, and Arg23 on TP4 are required for the interaction. TP4 treatment in A549 cells was found to disrupt the microtubule network in cells, and mutation of the essential TP4 residues prevented microtubule depolymerization in vitro. Importantly, the TP4 mutants also showed decreased cytotoxicity in A549 cells, suggesting that microtubule disruption is a major mechanistic component of TP4-mediated death in lung carcinoma cells. View Full-Text
Keywords: antimicrobial peptide (AMP); tilapia piscidin 4 (TP4); microtubule antimicrobial peptide (AMP); tilapia piscidin 4 (TP4); microtubule

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Ting, C.-H.; Liu, Y.-C.; Lyu, P.-C.; Chen, J.-Y. Nile Tilapia Derived Antimicrobial Peptide TP4 Exerts Antineoplastic Activity Through Microtubule Disruption. Mar. Drugs 2018, 16, 462.

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