Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo

Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo

TRPA1 is a homotetrameric non-selective calcium-permeable channel. It contributes to chemical and temperature sensitivity, acute pain sensation, and development of inflammation. HCIQ2c1 is a peptide from the sea anemone <i>Heteractis magnifica</i> that inhibits serine proteases. Here, we...

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Bibliographic Details
Main Authors: Aleksandra N. Kvetkina, Sergey D. Oreshkov, Pavel A. Mironov, Maxim M. Zaigraev, Anna A. Klimovich, Yulia V. Deriavko, Aleksandr S. Menshov, Dmitrii S. Kulbatskii, Yulia A. Logashina, Yaroslav A. Andreev, Anton O. Chugunov, Mikhail P. Kirpichnikov, Ekaterina N. Lyukmanova, Elena V. Leychenko, Zakhar O. Shenkarev
Format: Article
Language:English
Published: MDPI AG 2024-12-01
Series:Marine Drugs
Subjects:
Kunitz-peptide
sea anemone
TRPA1
pain
nociceptive reaction
in vivo
Online Access:https://www.mdpi.com/1660-3397/22/12/542

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https://www.mdpi.com/1660-3397/22/12/542

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