Conformational structural changes of bacteriorhodopsin adsorbed onto single-walled carbon nanotubes.
The interaction between purple membranes, composed of proteins of bacteriorhodopsin (bR) and their native surrounding lipids, and single-walled carbon nanotubes (SWNT) has been investigated. In this work, sonication has been used to debundle SWNT in buffer solution without surfactant before the addition of native purple membranes. The sample was then sonicated in a bath for a short time, followed by a centrifugation. The supernatants contain proteins in excess and SWNT as individual and small bundles covered by a bR layer with an average thickness of 1.5 nm. TEM and AFM observations support the idea that only a protein monolayer surrounds the tubes. Optical absorption and infrared spectroscopy measurements provide evidence that the proteins adsorbed onto the SWNT undergo orientational changes of the helical segments in bR and helix conformational changes. We ascribe the main driving force to the hydrophobic interactions between the sidewall of the SWNT and the hydrophobic residues of the alpha-helices of bR.
Bertoncini
Patricia
P
Institut des Matériaux Jean Rouxel, Nantes Université, CNRS, France. Patricia.Bertoncini@cnrs-imn.fr
Chauvet
Olivier
O
D001436:Bacteriorhodopsins / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D037742:Nanotubes, Carbon; D011487:Protein Conformation; D017550:Spectroscopy, Fourier Transform Infrared
D037742:Nanotubes, Carbon; D001436:Bacteriorhodopsins