Anti-Microbial and Anti-Cancer Properties of Tat-IV13, A Hybrid Bi-Partite Peptide Containing The Short Non Active Iv13 Sequence of Human Ll37 Cathelecidin

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Author Info

Alphonse Garcia Bruno Périchon

Corresponding Author

Alphonse Garcia
Laboratoire E3 des Phosphatases-Unité RMN

A B S T R A C T

Therapeutic strategies based on optimization of the unique human LL37 cathelecin sequences including FK16, the core active sequence of LL37, have already been proposed. In this study we have characterized TatIV13 a new host defense hybrid peptide, that combined YGRRKKRRQRRR, the hydrophobic N-terminal fragment of HIV-1 Tat47-57 cell penetrating sequence, with IV13, a short IVQRIKDFLRNLV inactive sequence resulting from the deletion of the three N-terminal amino acid residues of FK16. Tat- IV13 displayed potent host defense inhibitory effects leading both to the survival inhibition of U87G cells, a glioblastoma model, and to the inhibition of the growth of S. agalactiae NEM316 ΔdltA strain, a Gram+ bacterial model. These results suggest that identification of hybrid specific Tat-cathelecidin peptides with high anti-tumor activity and anti-bactericidal activity may represent a powerful approach to identify new candidates for future therapeutic developments.

Article Info

Article Type

Research Article

Publication history

Received: Sun 08, Sep 2019
Accepted: Thu 31, Oct 2019
Published: Thu 05, Dec 2019

Copyright

© 2023 Alphonse Garcia. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Hosting by Science Repository.
DOI: 10.31487/j.CMR.2019.01.03