Next Article in Journal
Ceratinadins E and F, New Bromotyrosine Alkaloids from an Okinawan Marine Sponge Pseudoceratina sp.
Previous Article in Journal
Fucoidan Extracted from the New Zealand Undaria pinnatifida—Physicochemical Comparison against Five Other Fucoidans: Unique Low Molecular Weight Fraction Bioactivity in Breast Cancer Cell Lines
Article Menu

Export Article

Open AccessArticle
Mar. Drugs 2018, 16(12), 462; https://doi.org/10.3390/md16120462

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

1
Marine Research Station, Institute of Cellular and Organismic Biology, Academia Sinica, Ilan 262, Taiwan
2
Institute of Population Sciences, National Health Research Institutes, Zhunan 350, Taiwan
3
Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsinchu 300, Taiwan
4
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
Full-Text   |   PDF [6037 KB, uploaded 22 November 2018]   |  

Abstract

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
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material

SciFeed

Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top