TanP: A Multifunctional Anionic Peptide From Tityus stigmurus Scorpion Venom
Anionic peptides of scorpions are molecules rich in aspartic and/or glutamic acid residues and correspond to a class of peptides without disulfide bonds that are still little explored. TanP is a linear anionic peptide (50 amino acid residues and net charge -20) present in the venom gland of the scor...
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Published in | Frontiers in molecular biosciences Vol. 8; p. 785316 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
Frontiers Media S.A
17.01.2022
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Subjects | |
Online Access | Get full text |
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Summary: | Anionic peptides of scorpions are molecules rich in aspartic and/or glutamic acid residues and correspond to a class of peptides without disulfide bonds that are still little explored. TanP is a linear anionic peptide (50 amino acid residues and net charge -20) present in the venom gland of the scorpion,
, with chelating properties for Cu
ion and immunomodulatory properties. The therapeutic application of chelating molecules is related to cases of acute or chronic intoxication by metals, neurodegenerative diseases, hematological diseases, healing of skin wounds, cardiovascular diseases, and cancer. In this approach, the chelating activity of TanP was evaluated in relation to new metal ions (Fe
and Zn
) of biological importance, as well as its antioxidant, hemostatic, immunomodulatory, and healing potential, aiming to expand the biological and biotechnological potential of this peptide. TanP (25 µM) was able to form stable complexes with Fe
in a ratio of 1:5 (TanP: Fe
). Theoretical results suggest that TanP can work as a sensor to identify and quantify Fe
ions. The fluorescence intensity of TanP (1.12 µM) decreased significantly after the addition of Fe
, obtaining the highest ratio 1: 7.4 (TanP: Fe
) that led to the lowest fluorescence intensity. For Zn
, no relevant spectral change was noted. TanP (50 µM) showed a maximum of 3% of hemolytic activity, demonstrating biocompatibility, as well as exhibiting a 1,1-diphenyl-2-picrylhydrazyl radical-scavenging activity of above 70% at all the concentrations tested (1-25 μM), and 89.7% iron-chelating activity at 25 μM and 96% hydroxyl radical-scavenging activity at 73.6 μM. In addition, TanP (12.5 and 25 µM) revealed an anticoagulant effect, prolonging the clotting time in prothrombin time and activated partial thromboplastin time assays, with no fibrinogenolytic activity. TanP (12.5 and 25 µM) induced the release of TNF-α by murine macrophages, in the absence of lipopolysaccharides, with a concentration-dependent increase and also stimulated the migration of 3T3 cells in the
healing assay. Thus, TanP revealed a multifunctional potential, being useful as a prototype for the development of new therapeutic and biotechnological agents. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Edited by: Maria Elena De Lima, Grupo Santa Casa BH, Brazil Thiago Verano-Braga, Federal University of Minas Gerais, Brazil Rodrigo Moreira Verly, Universidade Federal dos Vales do Jequitinhonha e Mucuri (UFVJM), Brazil Reviewed by: Juliana Carvalho Tavares, Federal University of Minas Gerais, Brazil This article was submitted to Cellular Biochemistry, a section of the journal Frontiers in Molecular Biosciences |
ISSN: | 2296-889X 2296-889X |
DOI: | 10.3389/fmolb.2021.785316 |