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Toxins 2018, 10(8), 320; https://doi.org/10.3390/toxins10080320

Biological Activities of Cationicity-Enhanced and Hydrophobicity-Optimized Analogues of an Antimicrobial Peptide, Dermaseptin-PS3, from the Skin Secretion of Phyllomedusa sauvagii

1
Natural Drug Discovery Group, School of Pharmacy, Queen’s University Belfast, Belfast BT9 7BL, Northern Ireland, UK
2
Faculty of Health Sciences, University of Macau, Avenida de Universidade, Taipa, Macau, China
*
Authors to whom correspondence should be addressed.
Received: 4 July 2018 / Revised: 28 July 2018 / Accepted: 3 August 2018 / Published: 7 August 2018
(This article belongs to the Special Issue Venom and Toxin as Targeted Therapy)
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Abstract

The skin secretions of the subfamily Phyllomedusinae have long been known to contain a number of compounds with antimicrobial potential. Herein, a biosynthetic dermaseptin-precursor cDNA was obtained from a Phyllomedusa sauvagii skin secretion-derived cDNA library, and thereafter, the presence of the mature peptide, namely dermaseptin-PS3 (DPS3), was confirmed by LC–MS/MS. Moreover, this naturally occurring peptide was utilized to design two analogues, K5, 17-DPS3 (introducing two lysine residues at positions 5 and 17 to replace acidic amino acids) and L10, 11-DPS3 (replacing two neutral amino acids with the hydrophobic amino acid, leucine), improving its cationicity on the polar/unipolar face and hydrophobicity in a highly conserved sequence motif, respectively. The results in regard to the two analogues show that either increasing cationicity, or hydrophobicity, enhance the antimicrobial activity. Also, the latter analogue had an enhanced anticancer activity, with pretreatment of H157 cells with 1 µM L10, 11-DPS3 decreasing viability by approximately 78%, even though this concentration of peptide exhibited no haemolytic effect. However, it must be noted that in comparison to the initial peptide, both analogues demonstrate higher membrane-rupturing capacity towards mammalian red blood cells. View Full-Text
Keywords: antimicrobial peptide (AMP); dermaseptin; anuran skin secretion; drug design; antimicrobial activity; anticancer activity antimicrobial peptide (AMP); dermaseptin; anuran skin secretion; drug design; antimicrobial activity; anticancer activity
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Tan, Y.; Chen, X.; Ma, C.; Xi, X.; Wang, L.; Zhou, M.; Burrows, J.F.; Kwok, H.F.; Chen, T. Biological Activities of Cationicity-Enhanced and Hydrophobicity-Optimized Analogues of an Antimicrobial Peptide, Dermaseptin-PS3, from the Skin Secretion of Phyllomedusa sauvagii. Toxins 2018, 10, 320.

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