A Novel Antimicrobial Peptide, Dermaseptin-SS1, with Anti-Proliferative Activity, Isolated from the Skin Secretion of Phyllomedusa tarsius

Xiaonan Ma; Yuping Chen; Anmei Shu; Yangyang Jiang; Xiaoling Chen; Chengbang Ma; Mei Zhou; Tao Wang; Tianbao Chen; Chris Shaw; Lei Wang

doi:10.20944/preprints202308.0727.v1

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preprints.org > biology and life sciences > biology and biotechnology > doi: 10.20944/preprints202308.0727.v1

Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

A Novel Antimicrobial Peptide, Dermaseptin-SS1, with Anti-Proliferative Activity, Isolated from the Skin Secretion of Phyllomedusa tarsius

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Version 1 : Received: 3 August 2023 / Approved: 9 August 2023 / Online: 9 August 2023 (10:45:09 CEST)

A peer-reviewed article of this Preprint also exists.

Ma, X.; Chen, Y.; Shu, A.; Jiang, Y.; Chen, X.; Ma, C.; Zhou, M.; Wang, T.; Chen, T.; Shaw, C.; Wang, L. A Novel Antimicrobial Peptide, Dermaseptin-SS1, with Anti-Proliferative Activity, Isolated from the Skin Secretion of Phyllomedusa tarsius. Molecules 2023, 28, 6558. Ma, X.; Chen, Y.; Shu, A.; Jiang, Y.; Chen, X.; Ma, C.; Zhou, M.; Wang, T.; Chen, T.; Shaw, C.; Wang, L. A Novel Antimicrobial Peptide, Dermaseptin-SS1, with Anti-Proliferative Activity, Isolated from the Skin Secretion of Phyllomedusa tarsius. Molecules 2023, 28, 6558.

Abstract

The emergence of multi-drug resistant bacteria has severely increased the burden on the global health system, and such pathogen infections are considered a great threat to human well-being. Antimicrobial peptides, due to their potent antimicrobial activity and low possibility of inducing resistance, are increasingly becoming the focus of much interest. Herein, a novel dermaseptin peptide, named Dermaseptin-SS1 (SS1), was identified from a skin secretion-derived cDNA library of the South/Central American tarsier leaf frog, Phyllomedusa tarsius, using a ‘shotgun’ cloning strategy. Chemically-synthesised peptide SS1 was found to be broadly effective against Gram-negative bacteria with low haemolytic activity in vitro. A designed synthetic analogue of SS1, named peptide 14V5K, showed a lower salt sensitivity with more rapid bacteria-killing compared to SS1. Both peptides employed the membrane-targeting mechanism to kill Escherichia coli. The antiproliferative activity of SS1 and its analogues, against lung cancer cell lines, was found to be significant.

Keywords

antimicrobial peptide; dermaseptin; molecular cloning; analogue design

Subject

Biology and Life Sciences, Biology and Biotechnology

Copyright: 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.

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