HIV fusion; glycoprotein; second harmonic generation; non linear optics
Abstract :
[en] The glycoprotein gp41 from the Human Immunodeficiency Virus type 1 (HIV-1) has an amino acid sequence enriched in tryptophan residues, the so-called gp41W peptide (i.e., KWASLWNWFNITNWLWYIK) and plays a crucial role in HIV-1 host cell infection. Using the coupling of Second Harmonic Generation targeting the tryptophan residues with lateral surface tension measurements, we investigate the interaction of gp41W with a neat air/water and a lipid/water interfaces. At the air/water interface, gp41W presents a well-defined orientation and this orientation is strongly modified at the lipid/water interface, depending on the surface pressure. These results show that this strategy is well suited to monitor tryptophan containing α-helices orientation at lipid/water interfaces.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Matar, Gladys
Benichou, Emmanuel
Nasir, Mehmet Nail ; Université de Liège - ULiège > Chimie et bio-industries > Chimie générale et organique
El Harfouch, Yara
Brevet, Pierre-François
Besson, Françoise
Language :
English
Title :
Reorientation of the helix of the tryptophan-rich gp41W peptide from HIV-1 at interfaces
Publication date :
December 2013
Journal title :
Journal of Chemical Physics
ISSN :
0021-9606
eISSN :
1089-7690
Publisher :
American Institute of Physics, New York, United States - New York
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