Academic Journal
Analogs of the scorpion venom peptide Stigmurin ; Structural assessment, toxicity, and increased antimicrobial activity
| العنوان: | Analogs of the scorpion venom peptide Stigmurin ; Structural assessment, toxicity, and increased antimicrobial activity |
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| المؤلفون: | Adriana M.S., Parente, Alessandra, Daniele-Silva, Allanny Alves, Furtado, Marcella Martins A., Melo, Ariane Ferreira, Lacerda, Moacir Fernandes, Queiroz, Moreno, Claudia Jassica Gonçalves, Elizabeth C.G., Santos, Hugo Alexandre Oliveira, Rocha, Euzébio Guimarães, Barbosa, Enéas De, Carvalho, Arnóbio Antônio Da, Silva-Júnior, Silva, MS, Matheus De Freitas, Fernandes-Pedrosa, Matheus De Freitas |
| المساهمون: | Instituto de Higiene e Medicina Tropical (IHMT), Global Health and Tropical Medicine (GHTM), Vector borne diseases and pathogens (VBD) |
| سنة النشر: | 2018 |
| المجموعة: | Repositório da Universidade Nova de Lisboa (UNL) |
| مصطلحات موضوعية: | Stigmurin, Analog peptides, Antimicrobial peptides, Antiparasitic, Antiproliferative, Scorpion venom, Structure-activity relationships, SDG 3 - Good Health and Well-being |
| الوصف: | 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. ; publishersversion ; published |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 2072-6651 |
| Relation: | PURE: 6182031; PURE UUID: 0434cec5-da7c-4cbb-a767-4eaac36582f2; Scopus: 85047125175; PubMed: 29670004; PubMedCentral: PMC5923327; http://hdl.handle.net/10362/116857; https://doi.org/10.3390/toxins10040161 |
| DOI: | 10.3390/toxins10040161 |
| الاتاحة: | http://hdl.handle.net/10362/116857 https://doi.org/10.3390/toxins10040161 |
| Rights: | openAccess |
| رقم الانضمام: | edsbas.A1D91402 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 20726651 |
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| DOI: | 10.3390/toxins10040161 |