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Open AccessArticle

Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin

1
Laboratory of Pharmaceutical Technology and Biotechnology, Pharmacy Department, Federal University of Rio Grande do Norte, Natal, Rio Grande do Norte 59012-570, Brazil
2
Laboratory of Bacteriology, Instituto Butantan, São Paulo 05503-900, Brazil
3
Immunoparasitology Laboratory, Department of Clinical and Toxicological Analysis, Federal University of Rio Grande do Norte, Natal 59012-570, Brazil
4
Global Health and Tropical Medicine, Institute of Hygiene and Tropical Medicine, Universidade Nova de Lisboa, 1099-085 Lisbon, Portugal
5
Brain Institute, Federal University of Rio Grande do Norte, Natal, Rio Grande do Norte 59056-340, Brazil
6
Analytical Chemistry and Chemical Physics Department, Federal University of Ceará, Fortaleza, Ceará 60455-900, Brazil
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(3), 623; https://doi.org/10.3390/ijms20030623
Received: 20 December 2018 / Revised: 22 January 2019 / Accepted: 24 January 2019 / Published: 31 January 2019
(This article belongs to the Section Biochemistry)
Scorpion venom constitutes a rich source of biologically active compounds with high potential for therapeutic and biotechnological applications that can be used as prototypes for the design of new drugs. The aim of this study was to characterize the structural conformation, evaluate the antimicrobial activity, and gain insight into the possible action mechanism underlying it, for two new analog peptides of the scorpion peptide Stigmurin, named StigA25 and StigA31. The amino acid substitutions in the native sequence for lysine residues resulted in peptides with higher positive net charge and hydrophobicity, with an increase in the theoretical helical content. StigA25 and StigA31 showed the capacity to modify their structural conformation according to the environment, and were stable to pH and temperature variation—results similar to the native peptide. Both analog peptides demonstrated broad-spectrum antimicrobial activity in vitro, showing an effect superior to that of the native peptide, being non-hemolytic at the biologically active concentrations. Therefore, this study demonstrates the therapeutic potential of the analog peptides from Stigmurin and the promising approach of rational drug design based on scorpion venom peptide to obtain new anti-infective agents. View Full-Text
Keywords: Tityus stigmurus; analog peptides; scorpion venom; antimicrobial agent; molecular dynamics; bacterial membrane Tityus stigmurus; analog peptides; scorpion venom; antimicrobial agent; molecular dynamics; bacterial membrane
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Amorim-Carmo, B.; Daniele-Silva, A.; Parente, A.M.S.; Furtado, A.A.; Carvalho, E.; Oliveira, J.W.F.; Santos, E.C.G.; Silva, M.S.; Silva, S.R.B.; Silva-Júnior, A.A.; Monteiro, N.K.; Fernandes-Pedrosa, M.F. Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin. Int. J. Mol. Sci. 2019, 20, 623.

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