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Toxins 2018, 10(4), 161; https://doi.org/10.3390/toxins10040161

Analogs of the Scorpion Venom Peptide Stigmurin: Structural Assessment, Toxicity, and Increased Antimicrobial Activity

1
Laboratório de Tecnologia e Biotecnologia Farmacêutica, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte 59010-115, Brazil
2
Programa de Pós-Graduação em Ciências Farmacêuticas, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte 59072-970, Brazil
3
Programa de Pós-Graduação em Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, Rio Grande do Norte 59072-970, Brazil
4
Instituto Butantan, São Paulo 05503-900, SP, Brazil
5
Global Health and Tropical Medicine, Institute of Hygiene and Tropical Medicine, Universidade Nova de Lisboa, 1099-085 Lisbon, Portugal
*
Author to whom correspondence should be addressed.
Received: 6 March 2018 / Revised: 7 April 2018 / Accepted: 14 April 2018 / Published: 18 April 2018
(This article belongs to the Special Issue Scorpion Toxins)
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Abstract

Scorpion venom is a rich source of biologically active components and various peptides with high-potential therapeutic use that have been characterized for their antimicrobial and antiproliferative activities. Stigmurin is a peptide identified from the Tityus stigmurus venom gland with high antibacterial and antiproliferative activities and low toxicity. Amino acid substitutions in peptides without a disulfide bridge sequence have been made with the aim of reducing their toxicity and increasing their biological activities. The purpose of this study was to evaluate the structural conformation and structural stability, as well as antimicrobial, antiproliferative, and hemolytic activities of two peptide analogs to Stigmurin, denominated StigA6 and StigA16. In silico analysis revealed the α-helix structure for both analog peptides, which was confirmed by circular dichroism. Data showed that the net charge and hydrophobic moment of the analog peptides were higher than those for Stigmurin, which can explain the increase in antimicrobial activity presented by them. Both analog peptides exhibited activity on cancerous cells similar to the native peptide; however, they were less toxic when tested on the normal cell line. These results reveal a potential biotechnological application of the analog peptides StigA6 and StigA16 as prototypes to new therapeutic agents. View Full-Text
Keywords: antimicrobial peptide; scorpion venom; antiproliferative; antiparasitic; structure-activity relationship; Stigmurin; analog peptides antimicrobial peptide; scorpion venom; antiproliferative; antiparasitic; structure-activity relationship; Stigmurin; analog peptides
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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).
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Parente, A.M.S.; Daniele-Silva, A.; Furtado, A.A.; Melo, M.A.; Lacerda, A.F.; Queiroz, M.; Moreno, C.; Santos, E.; Rocha, H.A.O.; Barbosa, E.G.; Carvalho, E.; Silva-Júnior, A.A.; Silva, M.S.; Fernandes-Pedrosa, M.F. Analogs of the Scorpion Venom Peptide Stigmurin: Structural Assessment, Toxicity, and Increased Antimicrobial Activity. Toxins 2018, 10, 161.

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