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Interaction of a peptide derived from C-terminus of human TRPA1 channel with model membranes mimicking the inner leaflet of the plasma membrane

dc.relation.isnodouble126070b1-3bea-4167-83db-9357a0e84f98*
dc.relation.isnodoubleb01b560f-b3c7-4d01-9f2f-5744f4929fdd*
dc.relation.isnodouble60369b3d-f1c0-40d8-a097-bda630dcb808*
dc.contributor.authorWITSCHAS, K.
dc.contributor.authorJOBIN, M. L.
dc.contributor.authorKORKUT, D. N.
dc.contributor.authorVLADAN, M. M.
dc.contributor.authorSALGADO, G.
dc.contributor.authorLECOMTE, S.
dc.contributor.authorVLACHOVA, V.
dc.contributor.authorD. ALVES, Isabel
dc.date.accessioned2020-09-03T08:01:56Z
dc.date.available2020-09-03T08:01:56Z
dc.date.issued2015
dc.identifier.issn0006-3002 (Print) 0006-3002
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10932
dc.description.abstractEnThe 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.
dc.language.isoen
dc.title.enInteraction of a peptide derived from C-terminus of human TRPA1 channel with model membranes mimicking the inner leaflet of the plasma membrane
dc.title.alternativeBiochimica et biophysica acta
dc.typeArticle de revue
dc.identifier.doi10.1016/j.bbamem.2015.02.003
dc.subject.halChimie/Matériaux
bordeaux.journalBiochim Biophys Acta
bordeaux.page1147-1156
bordeaux.volume1848
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue5
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochim%20Biophys%20Acta&rft.date=2015&rft.volume=1848&rft.issue=5&rft.spage=1147-1156&rft.epage=1147-1156&rft.eissn=0006-3002%20(Print)%200006-3002&rft.issn=0006-3002%20(Print)%200006-3002&rft.au=WITSCHAS,%20K.&JOBIN,%20M.%20L.&KORKUT,%20D.%20N.&VLADAN,%20M.%20M.&SALGADO,%20G.&rft.genre=article


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