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Updated: May 4, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
Reorientation of the helix of the tryptophan-rich gp41W peptide from HIV-1 at interfaces
Gladys Matar1, Emmanuel Benichou2, Mehmet Nail Nasir1
1Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, UMR CNRS 5246, CPE Lyon, INSA Lyon, Université Claude Bernard Lyon1, 43 Boulevard du 11 Novembre 1918, 69622 Villeurbanne cedex, France.
Abstract:
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.
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