Interaction of a peptide derived from C-terminus of human TRPA1 channel with model membranes mimicking the inner leaflet of the plasma membrane
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25687973
DOI
10.1016/j.bbamem.2015.02.003
PII: S0005-2736(15)00043-7
Knihovny.cz E-resources
- Keywords
- Conformation, Lipid-selective interaction, Peptide–lipid interactions, Secondary structure, TRP channels,
- MeSH
- Anisotropy MeSH
- Cell Membrane chemistry metabolism MeSH
- Transient Receptor Potential Channels chemistry metabolism MeSH
- TRPA1 Cation Channel MeSH
- Hydrogen-Ion Concentration MeSH
- Humans MeSH
- Membrane Lipids chemistry metabolism MeSH
- Membranes, Artificial * MeSH
- Nuclear Magnetic Resonance, Biomolecular MeSH
- Peptide Fragments chemistry metabolism MeSH
- Nerve Tissue Proteins chemistry metabolism MeSH
- Buffers MeSH
- Protein Folding MeSH
- Protein Structure, Secondary MeSH
- Protein Structure, Tertiary MeSH
- Calcium Channels chemistry metabolism MeSH
- Protein Binding MeSH
- Structure-Activity Relationship MeSH
- Phase Transition MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Transient Receptor Potential Channels MeSH
- TRPA1 Cation Channel MeSH
- Membrane Lipids MeSH
- Membranes, Artificial * MeSH
- Peptide Fragments MeSH
- Nerve Tissue Proteins MeSH
- Buffers MeSH
- TRPA1 protein, human MeSH Browser
- Calcium Channels 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
References provided by Crossref.org
Transient receptor potential ankyrin 1 channel: An evolutionarily tuned thermosensor
