Use of the quartz crystal microbalance to monitor ligand-induced conformational rearrangements in HIV-1 envelope protein gp120.
We evaluated the potential of a quartz crystal microbalance with dissipation monitoring (QCM-D) to provide a sensitive, label-free method for detecting the conformational rearrangement of glycoprotein gp120 upon binding to different ligands. This glycoprotein is normally found on the envelope of the HIV-1 virus and is involved in viral entry into host cells. It was immobilized on the surface of the sensing element of the QCM-D and was exposed to individual solutions of several different small-molecule inhibitors as well as to a solution of a soluble form of the host cell receptor to which gp120 binds. Instrument responses to ligand-triggered changes were in qualitative agreement with conformational changes as suggested by other biophysical methods.
Lee
Hyun-Su
HS
Department of Chemistry, Drexel University, 3141 Chestnut Street, Philadelphia, PA 19104, USA.
Contarino
Mark
M
Umashankara
M
M
Schön
Arne
A
Freire
Ernesto
E
Smith
Amos B
AB
Chaiken
Irwin M
IM
Penn
Lynn S
LS
D002623:Chemistry Techniques, Analytical / Q000379:methods*; D015699:HIV Envelope Protein gp120 / Q000032:analysis* / Q000378:metabolism*; D015497:HIV-1 / Q000378:metabolism*; D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation; D011791:Quartz
D015699:HIV Envelope Protein gp120; D008024:Ligands; C514793:gp120 protein, Human immunodeficiency virus 1; D011791:Quartz