Novel neuroprotective peptides in the venom of the solitary scoliid wasp
Comprehensive analysis
LC-ESI-MS
Neuroprotective peptide
Solitary wasp
Venom
Journal
The journal of venomous animals and toxins including tropical diseases
ISSN: 1678-9199
Titre abrégé: J Venom Anim Toxins Incl Trop Dis
Pays: Brazil
ID NLM: 101201501
Informations de publication
Date de publication:
11 Jun 2021
11 Jun 2021
Historique:
entrez:
1
7
2021
pubmed:
2
7
2021
medline:
2
7
2021
Statut:
epublish
Résumé
Solitary wasp venoms may be a rich source of neuroactive substances, since their venoms are used for paralyzing preys. We have been exploring bioactive constituents of solitary wasp venoms and, in this study, the component profile of the venom from a solitary scoliid wasp, A reverse-phase HPLC connected to ESI-MS was used for LC-MS analyses. Online mass fingerprinting was performed from TIC, and data-dependent tandem mass spectrometry gave the MS/MS spectra. The sequences of two major peptide components were determined by MALDI-TOF/TOF MS analysis, confirmed by solid phase synthesis. Using the synthetic peptides, biological activities were assessed. Cell integrity tests and neuroprotection analyzes using H Online mass fingerprinting revealed that the venom contains 123 components, and the MS/MS analysis resulted in 33 full sequences of peptide components. The two main peptides, α-scoliidine (DYVTVKGFSPLR) and β-scoliidine (DYVTVKGFSPLRKA), present homology with the bradykinin C-terminal. Despite this, both peptides did not behave as substrates or inhibitors of ACE, indicating that they do not interact with this metallopeptidase. In further studies, β-scoliidine, but not α -scoliidine, showed protective effects against oxidative stress-induced neurotoxicity in PC12 cells through integrity and metabolism cell assays. Interestingly, β-scoliidine has the extension of the KA dipeptide at the C-terminal in comparison with α-scoliidine. Comprehensive LC-MS and MS/MS analyses from the
Sections du résumé
BACKGROUND
BACKGROUND
Solitary wasp venoms may be a rich source of neuroactive substances, since their venoms are used for paralyzing preys. We have been exploring bioactive constituents of solitary wasp venoms and, in this study, the component profile of the venom from a solitary scoliid wasp,
METHODS
METHODS
A reverse-phase HPLC connected to ESI-MS was used for LC-MS analyses. Online mass fingerprinting was performed from TIC, and data-dependent tandem mass spectrometry gave the MS/MS spectra. The sequences of two major peptide components were determined by MALDI-TOF/TOF MS analysis, confirmed by solid phase synthesis. Using the synthetic peptides, biological activities were assessed. Cell integrity tests and neuroprotection analyzes using H
RESULTS
RESULTS
Online mass fingerprinting revealed that the venom contains 123 components, and the MS/MS analysis resulted in 33 full sequences of peptide components. The two main peptides, α-scoliidine (DYVTVKGFSPLR) and β-scoliidine (DYVTVKGFSPLRKA), present homology with the bradykinin C-terminal. Despite this, both peptides did not behave as substrates or inhibitors of ACE, indicating that they do not interact with this metallopeptidase. In further studies, β-scoliidine, but not α -scoliidine, showed protective effects against oxidative stress-induced neurotoxicity in PC12 cells through integrity and metabolism cell assays. Interestingly, β-scoliidine has the extension of the KA dipeptide at the C-terminal in comparison with α-scoliidine.
CONCLUSION
CONCLUSIONS
Comprehensive LC-MS and MS/MS analyses from the
Identifiants
pubmed: 34194483
doi: 10.1590/1678-9199-JVATITD-2020-0171
pmc: PMC8215932
doi:
Types de publication
Journal Article
Langues
eng
Pagination
e20200171Déclaration de conflit d'intérêts
Competing interests: The authors declare that they have no competing interests.
Références
Front Oncol. 2014 Sep 16;4:249
pubmed: 25279352
Toxicon. 1987;25(5):527-35
pubmed: 3617088
Toxins (Basel). 2016 Apr 18;8(4):114
pubmed: 27096870
J Exp Med. 1995 Nov 1;182(5):1469-79
pubmed: 7595217
Biochem Biophys Res Commun. 2005 May 20;330(4):1048-54
pubmed: 15823549
Drug Des Devel Ther. 2019 Jul 03;13:2067-2079
pubmed: 31308624
Toxicon. 2001 Aug;39(8):1257-60
pubmed: 11306139
Toxicon. 2019 Feb;158:109-126
pubmed: 30543821
Toxicon. 2002 Mar;40(3):309-12
pubmed: 11711128
Biomed Pharmacother. 2017 Jul;91:162-166
pubmed: 28463790
DNA Cell Biol. 2017 Jul;36(7):518-528
pubmed: 28436683
Toxins (Basel). 2016 Jan 22;8(2):32
pubmed: 26805885
Toxins (Basel). 2019 Oct 10;11(10):
pubmed: 31658776
Cytometry A. 2015 Oct;87(10):929-35
pubmed: 26189685
Comp Biochem Physiol C Comp Pharmacol Toxicol. 1987;87(2):287-95
pubmed: 2888570
Comp Biochem Physiol C Comp Pharmacol Toxicol. 1990;96(1):157-62
pubmed: 1980872
Biochem Pharmacol. 2010 Feb 1;79(3):478-86
pubmed: 19716363
J Nutr Sci Vitaminol (Tokyo). 2005 Dec;51(6):398-405
pubmed: 16521698
Biochemistry. 2018 Mar 27;57(12):1907-1916
pubmed: 29350905
Toxins (Basel). 2019 Mar 10;11(3):
pubmed: 30857348
Neurochem Res. 2020 May;45(5):1034-1044
pubmed: 32016793
Oxid Med Cell Longev. 2012;2012:428010
pubmed: 22685618
J Neurochem. 2007 Jul;102(2):493-500
pubmed: 17403034
Toxins (Basel). 2020 Jan 25;12(2):
pubmed: 31991714
Cell Transplant. 2015;24(4):613-23
pubmed: 25839228
Molecules. 2019 Dec 07;24(24):
pubmed: 31817866
Fitoterapia. 2020 Mar;141:104472
pubmed: 31917303
Toxicon. 2015 Jan;93:125-35
pubmed: 25432067
FEBS Open Bio. 2017 Feb 20;7(4):485-494
pubmed: 28396834
Mol Neurobiol. 2019 Jun;56(6):4023-4036
pubmed: 30259399
Toxicon. 2019 Sep;167:29-37
pubmed: 31181294
Toxins (Basel). 2019 Sep 24;11(10):
pubmed: 31554187
Peptides. 2018 May;103:90-97
pubmed: 29605732
Cold Spring Harb Protoc. 2016 Apr 01;2016(4):pdb.prot087379
pubmed: 27037069
Mutat Res. 2017 Jul;773:274-281
pubmed: 28927535
Toxins (Basel). 2015 Aug 18;7(8):3179-209
pubmed: 26295258
Mol Neurobiol. 2014 Aug;50(1):186-96
pubmed: 24436056
Biochem Biophys Res Commun. 1998 Sep 29;250(3):612-6
pubmed: 9784394
Curr Neurovasc Res. 2005 Jan;2(1):73-89
pubmed: 16181101