title: Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.
abstract: Membrane binding of proteins such as short chain dehydrogenase reductases or tail-anchored proteins relies on their N- and/or C-terminal hydrophobic transmembrane segment. In this review, we propose guidelines to characterize such hydrophobic peptide segments using spectroscopic and biophysical measurements. The secondary structure content of the C-terminal peptides of retinol dehydrogenase 8, RGS9-1 anchor protein, lecithin retinol acyl transferase, and of the N-terminal peptide of retinol dehydrogenase 11 has been deduced by prediction tools from their primary sequence as well as by using infrared or circular dichroism analyses. Depending on the solvent and the solubilization method, significant structural differences were observed, often involving α-helices. The helical structure of these peptides was found to be consistent with their presumed membrane binding. Langmuir monolayers have been used as membrane models to study lipid-peptide interactions. The values of maximum insertion pressure obtained for all peptides using a monolayer of 1,2-dioleoyl-sn-glycero-3-phospho-ethanolamine (DOPE) are larger than the estimated lateral pressure of membranes, thus suggesting that they bind membranes. Polarization modulation infrared reflection absorption spectroscopy has been used to determine the structure and orientation of these peptides in the absence and in the presence of a DOPE monolayer. This lipid induced an increase or a decrease in the organization of the peptide secondary structure. Further measurements are necessary using other lipids to better understand the membrane interactions of these peptides.
authors.affiliation: CUO-Recherche, Centre de recherche du CHU de Québec, Hôpital du Saint-Sacrement, Département d'ophtalmologie, Faculté de médecine, Université Laval, Québec, Québec G1V 0A6, Canada; Regroupement stratégique PROTEO, Université Laval, Québec, Québec G1V 0A6, Canada.
authors.forename: Mustapha
authors.initials: M
authors.lastname: Lhor
authors.affiliation: CUO-Recherche, Centre de recherche du CHU de Québec, Hôpital du Saint-Sacrement, Département d'ophtalmologie, Faculté de médecine, Université Laval, Québec, Québec G1V 0A6, Canada; Regroupement stratégique PROTEO, Université Laval, Québec, Québec G1V 0A6, Canada.
authors.forename: Sarah C
authors.initials: SC
authors.lastname: Bernier
authors.affiliation: CUO-Recherche, Centre de recherche du CHU de Québec, Hôpital du Saint-Sacrement, Département d'ophtalmologie, Faculté de médecine, Université Laval, Québec, Québec G1V 0A6, Canada; Regroupement stratégique PROTEO, Université Laval, Québec, Québec G1V 0A6, Canada.
authors.forename: Habib
authors.initials: H
authors.lastname: Horchani
authors.affiliation: CUO-Recherche, Centre de recherche du CHU de Québec, Hôpital du Saint-Sacrement, Département d'ophtalmologie, Faculté de médecine, Université Laval, Québec, Québec G1V 0A6, Canada; Regroupement stratégique PROTEO, Université Laval, Québec, Québec G1V 0A6, Canada.
authors.forename: Sylvain
authors.initials: S
authors.lastname: Bussières
authors.affiliation: CUO-Recherche, Centre de recherche du CHU de Québec, Hôpital du Saint-Sacrement, Département d'ophtalmologie, Faculté de médecine, Université Laval, Québec, Québec G1V 0A6, Canada; Regroupement stratégique PROTEO, Université Laval, Québec, Québec G1V 0A6, Canada.
authors.forename: Line
authors.initials: L
authors.lastname: Cantin
authors.affiliation: CBMN-UMR 5248 CNRS, Université de Bordeaux, IPB, Allée Geoffroy Saint Hilaire, 33600 Pessac, France.
authors.forename: Bernard
authors.initials: B
authors.lastname: Desbat
authors.affiliation: CUO-Recherche, Centre de recherche du CHU de Québec, Hôpital du Saint-Sacrement, Département d'ophtalmologie, Faculté de médecine, Université Laval, Québec, Québec G1V 0A6, Canada; Regroupement stratégique PROTEO, Université Laval, Québec, Québec G1V 0A6, Canada. Electronic address: Christian.Salesse@fmed.ulaval.ca.
authors.forename: Christian
authors.initials: C
authors.lastname: Salesse
mesh_terms: D000818:Animals; D055592:Biophysical Phenomena; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D010743:Phospholipids / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013499:Surface Properties
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins; D010446:Peptide Fragments; D010455:Peptides; D010743:Phospholipids
keywords: Circular dichroism and infrared spectroscopy; Lecithin retinol acyltransferase; Monolayer; R9AP; Retinol dehydrogenase; Transmembrane hydrophobic peptide