Interaction of a peptide derived from C-terminus of human TRPA1 channel with model membranes mimicking the inner leaflet of the plasma membrane
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25687973
DOI
10.1016/j.bbamem.2015.02.003
PII: S0005-2736(15)00043-7
Knihovny.cz E-zdroje
- Klíčová slova
- Conformation, Lipid-selective interaction, Peptide–lipid interactions, Secondary structure, TRP channels,
- MeSH
- anizotropie MeSH
- buněčná membrána chemie metabolismus MeSH
- kationtové kanály TRP chemie metabolismus MeSH
- kationtový kanál TRPA1 MeSH
- koncentrace vodíkových iontů MeSH
- lidé MeSH
- membránové lipidy chemie metabolismus MeSH
- membrány umělé * MeSH
- nukleární magnetická rezonance biomolekulární MeSH
- peptidové fragmenty chemie metabolismus MeSH
- proteiny nervové tkáně chemie metabolismus MeSH
- pufry MeSH
- sbalování proteinů MeSH
- sekundární struktura proteinů MeSH
- terciární struktura proteinů MeSH
- vápníkové kanály chemie metabolismus MeSH
- vazba proteinů MeSH
- vztahy mezi strukturou a aktivitou MeSH
- změna skupenství MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- kationtové kanály TRP MeSH
- kationtový kanál TRPA1 MeSH
- membránové lipidy MeSH
- membrány umělé * MeSH
- peptidové fragmenty MeSH
- proteiny nervové tkáně MeSH
- pufry MeSH
- TRPA1 protein, human MeSH Prohlížeč
- vápníkové kanály MeSH
The transient receptor potential ankyrin 1 channel (TRPA1) belongs to the TRP cation channel superfamily that responds to a panoply of stimuli such as changes in temperature, calcium levels, reactive oxygen and nitrogen species and lipid mediators among others. The TRP superfamily has been implicated in diverse pathological states including neurodegenerative disorders, kidney diseases, inflammation, pain and cancer. The intracellular C-terminus is an important regulator of TRP channel activity. Studies with this and other TRP superfamily members have shown that the C-terminus association with lipid bilayer alters channel sensitivity and activation, especially interactions occurring through basic residues. Nevertheless, it is not yet clear how this process takes place and which regions in the C-terminus would be responsible for such membrane recognition. With that in mind, herein the first putative membrane interacting region of the C-terminus of human TRPA1, (corresponding to a 29 residue peptide, IAEVQKHASLKRIAMQVELHTSLEKKLPL) named H1 due to its potential helical character was chosen for studies of membrane interaction. The affinity of H1 to lipid membranes, H1 structural changes occurring upon this interaction as well as effects of this interaction in lipid organization and integrity were investigated using a biophysical approach. Lipid models systems composed of zwitterionic and anionic lipids, namely those present in the lipid membrane inner leaflet, where H1 is prone to interact, where used. The study reveals a strong interaction and affinity of H1 as well as peptide structuration especially with membranes containing anionic lipids. Moreover, the interactions and peptide structure adoption are headgroup specific.
CBMN UMR 5248 CNRS University of Bordeaux IPB Allée Geoffroy St Hilaire 33600 Pessac France
INSERM U869 ARNA Laboratory University of Bordeaux 2 rue Robert Escarpit 33607 Pessac France
Citace poskytuje Crossref.org
Transient receptor potential ankyrin 1 channel: An evolutionarily tuned thermosensor
