Analgesic effects of Phα1β toxin: a review of mechanisms of action involving pain pathways

Analgesic effects of Phα1β toxin: a review of mechanisms of action involving pain pathways

Phα1β is a neurotoxin purified from spider venom that acts as a high-voltage-activated (HVA) calcium channel blocker. This spider peptide has shown a high selectivity for N-type HVA calcium channels (NVACC) and an analgesic effect in several animal models of pain. Its activity was associated with a...

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Published in:The journal of venomous animals and toxins including tropical diseases Vol. 27
Main Authors: Silva, Juliana Figueira da, Binda, Nancy Scardua, Pereira, Elizete Maria Rita, Lavor, Mário Sérgio Lima de, Vieira, Luciene Bruno, Souza, Alessandra Hubner de, Rigo, Flávia Karine, Ferrer, Hèlia Tenza, Castro Júnior, Célio José de, Ferreira, Juliano, Gomez, Marcus Vinicius
Format: Journal Article
Language:English
Published: Centro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESP 2021
Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
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Subjects:
Analgesia
CTK 01512-2
Pain
Phα1β peptide
Review
TOXICOLOGY
TROPICAL MEDICINE
TRPA1
Voltage-activated calcium channels
Analgesia
Pain
Voltage-activated calcium channels
Phα1β peptide
CTK 01512-2
TRPA1
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Abstract Phα1β is a neurotoxin purified from spider venom that acts as a high-voltage-activated (HVA) calcium channel blocker. This spider peptide has shown a high selectivity for N-type HVA calcium channels (NVACC) and an analgesic effect in several animal models of pain. Its activity was associated with a reduction in calcium transients, glutamate release, and reactive oxygen species production from the spinal cord tissue and dorsal ganglia root (DRG) in rats and mice. It has been reported that intrathecal (i.t.) administration of Phα1β to treat chronic pain reverted opioid tolerance with a safer profile than ω -conotoxin MVIIA, a highly selective NVACC blocker. Following a recent development of recombinant Phα1β (CTK 01512-2), a new molecular target, TRPA1, the structural arrangement of disulphide bridges, and an effect on glial plasticity have been identified. CTK 01512-2 reproduced the antinociceptive effects of the native toxin not only after the intrathecal but also after the intravenous administration. Herein, we review the Phα1β antinociceptive activity in the most relevant pain models and its mechanisms of action, highlighting the impact of CTK 01512-2 synthesis and its potential for multimodal analgesia.
AbstractList Abstract Phα1β is a neurotoxin purified from spider venom that acts as a high-voltage-activated (HVA) calcium channel blocker. This spider peptide has shown a high selectivity for N-type HVA calcium channels (NVACC) and an analgesic effect in several animal models of pain. Its activity was associated with a reduction in calcium transients, glutamate release, and reactive oxygen species production from the spinal cord tissue and dorsal ganglia root (DRG) in rats and mice. It has been reported that intrathecal (i.t.) administration of Phα1β to treat chronic pain reverted opioid tolerance with a safer profile than ω-conotoxin MVIIA, a highly selective NVACC blocker. Following a recent development of recombinant Phα1β (CTK 01512-2), a new molecular target, TRPA1, the structural arrangement of disulphide bridges, and an effect on glial plasticity have been identified. CTK 01512-2 reproduced the antinociceptive effects of the native toxin not only after the intrathecal but also after the intravenous administration. Herein, we review the Phα1β antinociceptive activity in the most relevant pain models and its mechanisms of action, highlighting the impact of CTK 01512-2 synthesis and its potential for multimodal analgesia.
Phα1β is a neurotoxin purified from spider venom that acts as a high-voltage-activated (HVA) calcium channel blocker. This spider peptide has shown a high selectivity for N-type HVA calcium channels (NVACC) and an analgesic effect in several animal models of pain. Its activity was associated with a reduction in calcium transients, glutamate release, and reactive oxygen species production from the spinal cord tissue and dorsal ganglia root (DRG) in rats and mice. It has been reported that intrathecal (i.t.) administration of Phα1β to treat chronic pain reverted opioid tolerance with a safer profile than ω -conotoxin MVIIA, a highly selective NVACC blocker. Following a recent development of recombinant Phα1β (CTK 01512-2), a new molecular target, TRPA1, the structural arrangement of disulphide bridges, and an effect on glial plasticity have been identified. CTK 01512-2 reproduced the antinociceptive effects of the native toxin not only after the intrathecal but also after the intravenous administration. Herein, we review the Phα1β antinociceptive activity in the most relevant pain models and its mechanisms of action, highlighting the impact of CTK 01512-2 synthesis and its potential for multimodal analgesia.
Author Gomez, Marcus Vinicius
Lavor, Mário Sérgio Lima de
Souza, Alessandra Hubner de
Vieira, Luciene Bruno
Ferrer, Hèlia Tenza
Ferreira, Juliano
Binda, Nancy Scardua
Pereira, Elizete Maria Rita
Castro Júnior, Célio José de
Rigo, Flávia Karine
Silva, Juliana Figueira da
AuthorAffiliation 5 Graduate Program in Health Sciences, University of the Extreme South of Santa Catarina (UNESC), Criciúma, SC, Brazil
2 Graduate Program in Health Sciences, Institute of Education and Research, Santa Casa de Belo Horizonte, Belo Horizonte, MG, Brazil
4 Department of Pharmacology, Institute of Biological Sciences (ICB), Federal University of Minas Gerais (UFMG), Belo Horizonte, MG, Brazil
6 Center of Technology in Molecular Medicine, School of Medicine, Federal University of Minas Gerais (UFMG), Belo Horizonte, MG, Brazil
3 Graduate Program in Animal Sciences, State University of Santa Cruz (UESC), Ilhéus, BA, Brazil
1 Laboratory of Pharmacology, Department of Pharmacy, Federal University of Ouro Preto, Ouro Preto, MG, Brazil
7 Department of Pharmacology, Federal University of Santa Catarina, Florianópolis, SC, Brazil
AuthorAffiliation_xml – name: 1 Laboratory of Pharmacology, Department of Pharmacy, Federal University of Ouro Preto, Ouro Preto, MG, Brazil
– name: 5 Graduate Program in Health Sciences, University of the Extreme South of Santa Catarina (UNESC), Criciúma, SC, Brazil
– name: 3 Graduate Program in Animal Sciences, State University of Santa Cruz (UESC), Ilhéus, BA, Brazil
– name: 7 Department of Pharmacology, Federal University of Santa Catarina, Florianópolis, SC, Brazil
– name: 2 Graduate Program in Health Sciences, Institute of Education and Research, Santa Casa de Belo Horizonte, Belo Horizonte, MG, Brazil
– name: 4 Department of Pharmacology, Institute of Biological Sciences (ICB), Federal University of Minas Gerais (UFMG), Belo Horizonte, MG, Brazil
– name: 6 Center of Technology in Molecular Medicine, School of Medicine, Federal University of Minas Gerais (UFMG), Belo Horizonte, MG, Brazil
– name: Institute of Education and Research, Santa Casa de Belo Horizonte
– name: Federal University of Minas Gerais
– name: Federal University of Santa Catarina
– name: Universidade Federal de Ouro Preto
– name: University of the Extreme South of Santa Catarina
– name: State University of Santa Cruz
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  givenname: Juliana Figueira da
  orcidid: 0000-0002-2906-517X
  surname: Silva
  fullname: Silva, Juliana Figueira da
  organization: Federal University of Ouro Preto, Brazil
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  givenname: Nancy Scardua
  surname: Binda
  fullname: Binda, Nancy Scardua
  organization: Federal University of Ouro Preto, Brazil
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  organization: Institute of Education and Research, Santa Casa de Belo Horizonte, Brazil
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  orcidid: 0000-0003-0795-5320
  surname: Lavor
  fullname: Lavor, Mário Sérgio Lima de
  organization: State University of Santa Cruz, Brazil
– sequence: 5
  givenname: Luciene Bruno
  orcidid: 0000-0002-3496-6749
  surname: Vieira
  fullname: Vieira, Luciene Bruno
  organization: Federal University of Minas Gerais, Brazil
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  givenname: Flávia Karine
  surname: Rigo
  fullname: Rigo, Flávia Karine
  organization: University of the Extreme South of Santa Catarina, Brazil
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  givenname: Hèlia Tenza
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  surname: Ferreira
  fullname: Ferreira, Juliano
  organization: Federal University of Santa Catarina, Brazil
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  givenname: Marcus Vinicius
  orcidid: 0000-0002-6082-930X
  surname: Gomez
  fullname: Gomez, Marcus Vinicius
  organization: Institute of Education and Research, Santa Casa de Belo Horizonte, Brazil; Federal University of Minas Gerais, Brazil
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Keywords Analgesia
Pain
Voltage-activated calcium channels
Phα1β peptide
CTK 01512-2
TRPA1
Language English
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Notes Competing interests: The authors declare that they have no competing interests.
Authors’ contributions: All the authors have contributed significantly to the execution, analyses, and writing of the study. All authors read and approved the final manuscript.
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PublicationTitle The journal of venomous animals and toxins including tropical diseases
PublicationTitleAlternate J. Venom. Anim. Toxins incl. Trop. Dis
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Snippet Phα1β is a neurotoxin purified from spider venom that acts as a high-voltage-activated (HVA) calcium channel blocker. This spider peptide has shown a high...
Abstract Phα1β is a neurotoxin purified from spider venom that acts as a high-voltage-activated (HVA) calcium channel blocker. This spider peptide has shown a...
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scielo
pubmedcentral
crossref
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Open Access Repository
Aggregation Database
SubjectTerms Analgesia
CTK 01512-2
Pain
Phα1β peptide
Review
TOXICOLOGY
TROPICAL MEDICINE
TRPA1
Voltage-activated calcium channels
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Title Analgesic effects of Phα1β toxin: a review of mechanisms of action involving pain pathways
URI https://pubmed.ncbi.nlm.nih.gov/PMC8610172
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