Evidence map›Paper›PMID 29663255›Full record

ArticleJournal of the American Society for Mass Spectrometry2018

Structural Characterization and Disulfide Assignment of Spider Peptide Phα1β by Mass Spectrometry.

Kelly L Wormwood, Armand Gatien Ngounou Wetie, Marcus Vinicius Gomez, Yue Ju, Paul Kowalski, Marius Mihasan, Costel C Darie

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Open veterinary journal · 2025
    Article
  4. Article
  5. Article
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  7. Article
  8. Article
  9. Article
  10. Analgesic effects of Phα1β toxin: a review of mechanisms of action involving pain pathways.The journal of venomous animals and toxins including tropical diseases · 2021
    Review
  11. Review
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Kelly L WormwoodBiochemistry & Proteomics Group, Department of Chemistry & Biomolecular Science, Clarkson University, 8 Clarkson Ave., Box 5810, Potsdam, NY, 13699, USA.
Armand Gatien Ngounou WetieBiochemistry & Proteomics Group, Department of Chemistry & Biomolecular Science, Clarkson University, 8 Clarkson Ave., Box 5810, Potsdam, NY, 13699, USA.
Marcus Vinicius GomezInstitute of Education and Research Santa Casa Belo Horizonte-Laboratory of Toxins, Rua Domingos Vieira 590, Belo Horizonte, Minas Gerais, 30150-240, Brazil.
Yue JuBruker Daltonics, 40 Manning Road Manning Park, Billerica, MA, 01821, USA.
Paul KowalskiBruker Daltonics, 40 Manning Road Manning Park, Billerica, MA, 01821, USA.
Marius MihasanBiochemistry & Proteomics Group, Department of Chemistry & Biomolecular Science, Clarkson University, 8 Clarkson Ave., Box 5810, Potsdam, NY, 13699, USA.
Costel C DarieBiochemistry & Proteomics Group, Department of Chemistry & Biomolecular Science, Clarkson University, 8 Clarkson Ave., Box 5810, Potsdam, NY, 13699, USA. cdarie@clarkson.edu.
Clarkson University · USBruker (United States) · USInsper · BR

Funding

ASPIRE Graduate Student Fellowship through Clarkson University's CUPO Office. ASPIRE Graduate Student Fellowship through Clarkson University's CUPO Office.
6 · The paper itself

Abstract

Native Phα1β is a peptide purified from the venom of the armed spider Phoneutria nigriventer that has been shown to have an extensive analgesic effect with fewer side effects than ω-conotoxin MVIIA. Recombinant Phα1β mimics the effects of the native Phα1β. Because of this, it has been suggested that Phα1β may have potential to be used as a therapeutic for controlling persistent pathological pain. The amino acid sequence of Phα1β is known; however, the exact structure and disulfide arrangement has yet to be determined. Determination of the disulfide linkages and exact structure could greatly assist in pharmacological analysis and determination of why this peptide is such an effective analgesic. Here, we used biochemical and mass spectrometry approaches to determine the disulfide linkages present in the recombinant Phα1β peptide. Using a combination of MALDI-MS, direct infusion ESI-MS, and nanoLC-MS/MS analysis of the undigested recombinant Phα1β peptide and digested with AspN, trypsin, or AspN/trypsin, we were able to identify and confirm all six disulfide linkages present in the peptide as Cys1-2, Cys3-4, Cys5-6, Cys7-8, Cys9-10, and Cys11-12. These results were also partially confirmed in the native Phα1β peptide. These experiments provide essential structural information about Phα1β and may assist in providing insight into the peptide's analgesic effect with very low side effects. Graphical Abstract ᅟ.

Indexed as

Amino Acid SequenceAnalgesicsAnimalsCysteineDisulfidesPeptidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSpidersSpider VenomsTandem Mass SpectrometryAnalgesicsCysteineDisulfidesPeptidesPhalpha1beta toxin, Phoneutria nigriventerSpider VenomsDisulfide bridgesMass spectrometryProtein structureVenom peptides

Identifiers

PMID29663255
OpenAlexW2801926006

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.