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NMR three-dimensional structure of the cationic peptide Stigmurin from Tityus stigmurus scorpion venom: In vitro antioxidant and in vivo antibacterial and healing activity.

Authors
  • Daniele-Silva, Alessandra1
  • Rodrigues, Suedson de Carvalho Silva2
  • Dos Santos, Elizabeth Cristina Gomes3
  • Queiroz Neto, Moacir Fernandes de4
  • Rocha, Hugo Alexandre de Oliveira4
  • Silva-Júnior, Arnóbio Antônio da1
  • Resende, Jarbas Magalhães5
  • Araújo, Renata Mendonça2
  • Fernandes-Pedrosa, Matheus de Freitas6
  • 1 Laboratório de Tecnologia e Biotecnologia Farmacêutica, Departamento de Farmácia, Universidade Federal do Rio Grande do Norte, Natal, Brazil. , (Brazil)
  • 2 Laboratório de Isolamento e Síntese de Compostos Orgânicos, Instituto de Química, Universidade Federal do Rio Grande do Norte, Natal, Brazil. , (Brazil)
  • 3 Laboratório de Imunoparasitologia. Departamento de Farmácia, Universidade Federal do Rio Grande do Norte, Natal, Brazil. , (Brazil)
  • 4 Laboratório de Biotecnologia de Polímeros Naturais, Departamento de Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, Brazil. , (Brazil)
  • 5 Laboratório de Síntese e Estrutura de Peptídeos, Departamento de Química, Universidade Federal de Minas Gerais, Belo Horizonte, Brazil. , (Brazil)
  • 6 Laboratório de Tecnologia e Biotecnologia Farmacêutica, Departamento de Farmácia, Universidade Federal do Rio Grande do Norte, Natal, Brazil. Electronic address: [email protected] , (Brazil)
Type
Published Article
Journal
Peptides
Publication Date
Jan 05, 2021
Volume
137
Pages
170478–170478
Identifiers
DOI: 10.1016/j.peptides.2020.170478
PMID: 33359395
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Infectious diseases and the rapid development of pathogens resistant to conventional drugs are a serious global public health problem, which motivates the search for new pharmacological agents. In this context, cationic peptides without disulfide bridges from different species of scorpion venom have been the target of scientific studies due to their multifunctional activities. Stigmurin is a linear peptide composed of 17 amino acid residues (Phe-Phe-Ser-Leu-Ile-Pro-Ser-Leu-Val-Gly-Gly-Leu-Ile-Ser-Ala-Phe-Lys-NH2), which is present in the venom gland of the scorpion Tityus stigmurus. Here we present investigations of the in vitro antioxidant action of Stigmurin together with the in vivo antibacterial and healing activity of this peptide in a wound infection model induced by Staphylococcus aureus. In addition, we have reports for the first time of the three-dimensional structure determined by NMR spectroscopy of a peptide without disulfide bridges present in scorpion venom from the Tityus genus. Stigmurin showed hydroxyl radical scavenging above 70 % at 10 μM and antibiotic action in the skin wound, reducing the number of viable microorganisms by 67.2 % on the 7 day after infection. Stigmurin (1 μg / μL) increased the retraction rate of the lesion, with wound area reduction of 43 % on the second day after skin injury, which indicates its ability to induce tissue repair. Stigmurin in trifluoroethanol:water exhibited a random conformation at the N-terminus region (Phe1 to Pro6), with a helical structure from Ser7 to Phe16. This structural information, allied with the multifunctional activity of Stigmurin, makes it an attractive candidate for the design of novel therapeutic agents. Copyright © 2020 Elsevier Inc. All rights reserved.

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