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    Use of the quartz crystal microbalance to monitor ligand-induced conformational rearrangements in HIV-1 envelope protein gp120

    Year: 2010

    Journal: Analytical and Bioanalytical Chemistry, Volume 396, Number 3 / February, 2010, Pages 1143-1152, 20100827

    Authors: Lee  H-S 1, Contarino M 2, Umashankara M. 2, Schön A. 3, Freire E. 3, Smith A.B. 4, Chaiken I.M. 2, Penn L.S. 1

    Last authors: Lynn S. Penn

    Organizations: (1) Department of Chemistry, Drexel University, 3141 Chestnut Street, Philadelphia, PA 19104, USA (2) Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, 245 N. 15th Street, Philadelphia, PA 19102, USA (3) Department of Biology, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA (4) Department of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, PA 19104, USA

    Country: USA, US, United States of America

    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.