Interaction with membranes of the full C-terminal domain of protein NS4B from Hepatitis C virus

Article ID	Journal	Published Year	Pages	File Type
10797267	Biochimica et Biophysica Acta (BBA) - Biomembranes	2012	14 Pages	PDF

Abstract

âº We have studied the binding and interaction of peptide NS4B_Cter from HCV NS4B with model membranes. âº Membrane lipid biophysical properties are modulated by NS4B_Cter. âº NS4B_Cter partitions into and interacts with membrane phospholipid membranes. âº NS4B_Cter structure is modulated by membrane binding. âº NS4B_cter region might be implicated in HCV replication process.

Keywords

TMA-DPH MLV DMPA NS4B TFE trifluoroethanol DPH DMPS DMPG EPA 5-Carboxyfluorescein N-palmitoyl-d-erythro-sphingosylphosphorylcholine bovine heart cardiolipin 1-(4-trimethylammoniumphenyl)-6-phenyl-1,3,5-hexatriene 5-NS 16-NS bovine brain l-α-phosphatidylserine egg l-α-phosphatidic acid BPI DSC CHOL EPC ESM TPE dMPC PSM BPS nuclear magnetic resonance 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine 1,6-diphenyl-1,3,5-hexatriene multilamellar vesicles egg sphingomyelin 16-doxyl-stearic acid 5-doxyl-stearic acid epg large unilamellar vesicles MAS egg l-α-phosphatidylcholine NMR Lipid–peptide interaction HCV replication magic angle spinning endoplasmic reticulum Lem LUV HCV Hepatitis C virus Non-structural protein Differential scanning calorimetry cholesterol