Article (Scientific journals)
Interfacial properties and structure stability of the gp41 tryptophan-rich peptide from HIV-1
Matar, Gladys; Nasir, Mehmet Nail; Besson, Françoise
2010In Journal of Colloid and Interface Science, 352, p. 520-525
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Abstract :
[en] The HIV-1 envelope glycoprotein 41 (gp41) undergoes large-scale conformational changes in order to induce the fusion of the virus and cell membranes. Thus, we investigated a possible structure transit at the air-water interface for the tryptophan-rich peptide of gp41 (gp41W). The synthetic peptide (KWASLWNWFNITNWLWYIK), corresponding to gp41W, shows interfacial properties on pure water and Tris buffer at pH 8.5. Isotherm measurements and Brewster angle microscopy (BAM) imaging showed that the behavior of the peptide monolayer was dependent on the subphase composition. A homogenous film was formed on buffer during the peptide monolayer compression, while the appearance of condensed domains on pure water could indicate the oligomerization of gp41W during the surface pressure increase. Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) showed that, whatever the subphase, gp41W adopts an α-helix structure at the air-water interface and does not transit for any other structure even at high surface pressures.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Matar, Gladys
Nasir, Mehmet Nail ;  Université de Liège - ULiège > Chimie et bio-industries > Chimie biologique industrielle
Besson, Françoise
Language :
English
Title :
Interfacial properties and structure stability of the gp41 tryptophan-rich peptide from HIV-1
Publication date :
2010
Journal title :
Journal of Colloid and Interface Science
ISSN :
0021-9797
eISSN :
1095-7103
Publisher :
Academic Press, Orlando, United States - Florida
Volume :
352
Pages :
520-525
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 15 March 2012

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