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

Laboratory of Pharmaceutical Technology and Biotechnology, Pharmacy Department, Federal University of Rio Grande do Norte, Natal, Rio Grande do Norte 59012-570, Brazil

Laboratory of Bacteriology, Instituto Butantan, São Paulo 05503-900, Brazil

Immunoparasitology Laboratory, Department of Clinical and Toxicological Analysis, Federal University of Rio Grande do Norte, Natal 59012-570, Brazil

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Global Health and Tropical Medicine, Institute of Hygiene and Tropical Medicine, Universidade Nova de Lisboa, 1099-085 Lisbon, Portugal

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Brain Institute, Federal University of Rio Grande do Norte, Natal, Rio Grande do Norte 59056-340, Brazil

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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)

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Abstract

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

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MDPI and ACS Style

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. https://doi.org/10.3390/ijms20030623

AMA Style

Amorim-Carmo B, Daniele-Silva A, Parente AMS, Furtado AA, Carvalho E, Oliveira JWF, Santos ECG, Silva MS, Silva SRB, Silva-Júnior AA, Monteiro NK, Fernandes-Pedrosa MF. Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin. International Journal of Molecular Sciences. 2019; 20(3):623. https://doi.org/10.3390/ijms20030623

Chicago/Turabian Style

Amorim-Carmo, Bruno, Alessandra Daniele-Silva, Adriana M. S. Parente, Allanny A. Furtado, Eneas Carvalho, Johny W. F. Oliveira, Elizabeth C. G. Santos, Marcelo S. Silva, Sérgio R. B. Silva, Arnóbio A. Silva-Júnior, Norberto K. Monteiro, and Matheus F. Fernandes-Pedrosa. 2019. "Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin" International Journal of Molecular Sciences 20, no. 3: 623. https://doi.org/10.3390/ijms20030623

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

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