TY - JOUR
T1 - Membrane de stabilization induced by the human immunodeficiency virus type-1 fusion peptide
AU - Nieva, José L.
AU - Goñi, Félix M.
AU - Muga, Arruro
AU - Nir, Shlomo
AU - Pereira, Francisca
PY - 1997
Y1 - 1997
N2 - The human immunodeficiency virus type-1 (HIV-1) fusion peptide, corresponding to a sequence of 23 amino acid residues at the N-terminus of the spike transmembrane subunit gp41, has the capacity to destabilize negatively charged and neutral large unilamellar vesicles, representing, respectively, the acidic and the neutral fraction of the plasma membrane lipids of viral target cells. As revealed by infrared spectroscopy, the peptide associated with the vesicles may exist in different conformations. In negatively charged membranes the structure is mainly an α-helix, while in Ca2+-neutralized negatively charged membranes the conformation switches to a predominantly extended conformation. In membranes composed of zwitterionic phospholipids and cholesterol, the peptide also adopts a predominant extended structure. The α-helical structure permeabilizes negatively charged vesicles but does not induce membrane fusion. The peptide in β-type conformation, on the other hand, permeabilizes neutral membranes and triggers fusion. As seen by 31P NMR, the latter structure also exhibits the capacity to alter the lamellar organization of the membrane.
AB - The human immunodeficiency virus type-1 (HIV-1) fusion peptide, corresponding to a sequence of 23 amino acid residues at the N-terminus of the spike transmembrane subunit gp41, has the capacity to destabilize negatively charged and neutral large unilamellar vesicles, representing, respectively, the acidic and the neutral fraction of the plasma membrane lipids of viral target cells. As revealed by infrared spectroscopy, the peptide associated with the vesicles may exist in different conformations. In negatively charged membranes the structure is mainly an α-helix, while in Ca2+-neutralized negatively charged membranes the conformation switches to a predominantly extended conformation. In membranes composed of zwitterionic phospholipids and cholesterol, the peptide also adopts a predominant extended structure. The α-helical structure permeabilizes negatively charged vesicles but does not induce membrane fusion. The peptide in β-type conformation, on the other hand, permeabilizes neutral membranes and triggers fusion. As seen by 31P NMR, the latter structure also exhibits the capacity to alter the lamellar organization of the membrane.
KW - Conformational switching
KW - Membrane fusion
KW - Peptide conformation
KW - Peptide-lipid interaction
UR - http://www.scopus.com/inward/record.url?scp=53249133256&partnerID=8YFLogxK
U2 - 10.1007/BF02442901
DO - 10.1007/BF02442901
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
AN - SCOPUS:53249133256
SN - 1573-3149
VL - 4
SP - 365
EP - 369
JO - International Journal of Peptide Research and Therapeutics
JF - International Journal of Peptide Research and Therapeutics
IS - 4-6
ER -