JBC INTERFERin siRNA transfection reagent

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Volume 271, Number 40, Issue of October 4, 1996 pp. 24617-24624
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Secondary and Tertiary Structure Changes of Reconstituted P-glycoprotein
A FOURIER TRANSFORM ATTENUATED TOTAL REFLECTION INFRARED SPECTROSCOPY ANALYSIS

(Received for publication, March 7, 1996, and in revised form, July 25, 1996)

Nathalie Sonveaux , Adam B. Shapiro § , Erik Goormaghtigh , Victor Ling § and Jean-Marie Ruysschaert

From the Laboratoire de Chimie Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, B-1050 Brussels, Belgium and the § British Columbia Cancer Research Centre, Vancouver, British Columbia, V5Z1L3 Canada

The structure of purified P-glycoprotein functionally reconstituted into liposomes was investigated by attenuated total reflection Fourier transform infrared spectroscopy. A quantitative evaluation of the secondary structure and a kinetic of 2H/H exchange of the P-glycoprotein were performed both in the presence and in the absence of MgATP, MgATP-verapamil, and MgADP. This approach was previously shown to be a useful tool to detect tertiary structure changes resulting from the interaction between a protein and its specific ligands, as established for the Neurospora crassa H+-ATPase.

2H/H exchange measurements provided evidence that a large fraction of the P-glycoprotein is poorly accessible to the aqueous medium. Addition of MgATP induced an increased accessibility to the solvent of a population of amino acids, while addition of MgATP-verapamil resulted in a subtraction of a part of the protein from access to the aqueous solvent. No significant changes were observed upon addition of MgADP or verapamil alone. The secondary structure of P-glycoprotein was not affected by addition of ligands. The variations observed in the 2H/H exchange rate when P-glycoprotein interacted with the above ligands therefore represented tertiary structure changes. Fluorescence quenching experiments confirmed that MgATP-induced changes are to be found in the tertiary structure of the enzyme.


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