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Protein & Cell is a copyright of Springer, 2017.

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.

Details

Title
Understand spiciness: mechanism of TRPV1 channel activation by capsaicin
Author
Yang, Fan; Zheng, Jie
Pages
169-177
Publication year
2017
Publication date
Jan 2017
Publisher
Springer Nature B.V.
ISSN
1674800X
e-ISSN
16748018
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
1871919631
Copyright
Protein & Cell is a copyright of Springer, 2017.