Understand spiciness: mechanism of TRPV1 channel activation by capsaicin
Protein & Cell
;
(12): 169-177, 2017.
Article
in English
| WPRIM
| ID: wpr-757338
ABSTRACT
Capsaicin in chili peppers bestows the sensation of spiciness. Since the discovery of its receptor, transient receptor potential vanilloid 1 (TRPV1) ion channel, how capsaicin activates this channel has been under extensive investigation using a variety of experimental techniques including mutagenesis, patch-clamp recording, crystallography, cryo-electron microscopy, computational docking and molecular dynamic simulation. A framework of how capsaicin binds and activates TRPV1 has started to merge capsaicin binds to a pocket formed by the channel's transmembrane segments, where it takes a "tail-up, head-down" configuration. Binding is mediated by both hydrogen bonds and van der Waals interactions. Upon binding, capsaicin stabilizes the open state of TRPV1 by "pull-and-contact" with the S4-S5 linker. Understanding the ligand-host interaction will greatly facilitate pharmaceutical efforts to develop novel analgesics targeting TRPV1.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Protein Binding
/
Binding Sites
/
Pharmacokinetics
/
Capsaicin
/
Chemistry
/
TRPV Cation Channels
/
Genetics
/
Hydrogen Bonding
/
Metabolism
Limits:
Humans
Language:
English
Journal:
Protein & Cell
Year:
2017
Type:
Article
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