TY - JOUR
T1 - Behaviour of a peptide sequence from the GB virus C/hepatitis G virus E2 protein in Langmuir monolayers
T2 - Its interaction with phospholipid membrane models
AU - Pérez-López, Silvia
AU - Nieto-Suárez, Marina
AU - Mestres, Concepció
AU - Alsina, M. Asunción
AU - Haro, Isabel
AU - Vila-Romeu, Nuria
N1 - Funding Information:
This work was supported by grants from the Ministerio de Ciencia e Innovación (Secretaría de Estado de Universidades, Dirección General de Programas y Transferencia de Conocimiento, Subdirección General de Proyectos de Investigación, Spain) CTQ 2006-15396-C02-01, CTQ 2006-15396-C02-02 and CTQ 2006-04085/BQU, and N. Vila-Romeu would also like to thank Xunta de Galicia for the grant of Rf. PGDIT06PXIB383004PR. The authors thank Rafael Zabala de Oleza for taking part in the synthesis of the studied peptide.
PY - 2009/5
Y1 - 2009/5
N2 - The GB virus C/hepatitis G virus (GBV C/HGV) is a Flaviviridae member that despite its non pathogenicity, has become of great interest given that it could inhibit the replication of the human immunodeficiency virus (HIV). Therefore, a better knowledge of the virus peptides involved in the cellular membrane fusion mechanism has become our aim. The selected peptide, named E2(347-363), corresponds to the GBV-C/HGV E2 protein and has been synthesized in order to study its interaction with in vitro membrane models. Two phospholipids, varying the charge and the unsaturations of the hydrocarbon chain have been chosen: 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DOPG). For our porpoise, we have used the Langmuir monolayer technique and Brewster angle microscopy (BAM) to gain deeper insight into the peptide/lipid interactions. The results obtained allow us to argue in favour of considering E2(347-363) a success candidate for developing further experiments in order to determine its potential role in the GBV C/HGV virus/cell membrane fusion process.
AB - The GB virus C/hepatitis G virus (GBV C/HGV) is a Flaviviridae member that despite its non pathogenicity, has become of great interest given that it could inhibit the replication of the human immunodeficiency virus (HIV). Therefore, a better knowledge of the virus peptides involved in the cellular membrane fusion mechanism has become our aim. The selected peptide, named E2(347-363), corresponds to the GBV-C/HGV E2 protein and has been synthesized in order to study its interaction with in vitro membrane models. Two phospholipids, varying the charge and the unsaturations of the hydrocarbon chain have been chosen: 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DOPG). For our porpoise, we have used the Langmuir monolayer technique and Brewster angle microscopy (BAM) to gain deeper insight into the peptide/lipid interactions. The results obtained allow us to argue in favour of considering E2(347-363) a success candidate for developing further experiments in order to determine its potential role in the GBV C/HGV virus/cell membrane fusion process.
KW - BAM
KW - Fusion peptide
KW - GBV-C/HGV
KW - Hepatitis G
KW - Membranes
KW - Phospholipid Langmuir monolayers
UR - http://www.scopus.com/inward/record.url?scp=62549106560&partnerID=8YFLogxK
U2 - 10.1016/j.bpc.2009.01.007
DO - 10.1016/j.bpc.2009.01.007
M3 - Article
C2 - 19232456
AN - SCOPUS:62549106560
SN - 0301-4622
VL - 141
SP - 153
EP - 161
JO - Biophysical Chemistry
JF - Biophysical Chemistry
IS - 2-3
ER -
