Role of the membrane interface on the conformation of the caveolin scaffolding domain: a CD and NMR study.
Circular dichroism (CD) and NMR spectroscopy were used to study the conformational properties of two synthetic peptides, D82-R101 and D82-I109, encompassing the caveolin scaffolding domain (D82-R101), in the presence of dodecylphosphocholine (DPC) micelles. Our data show that a stable helical conformation of the caveolin scaffolding domain in a membrane mimicking system is only obtained for the peptide including the L102-I109 hydrophobic stretch, a part of the caveolin intra-membrane domain. Through chemical shift variations, an ensemble of six residues of the D82-L109 peptide, mainly located in the V(94)TKYWFYR(101) motif were found to detect the presence of phosphatidylserine solubilized in DPC micelles. Our results constitute a first step for elucidating at a residue level the conformational properties of the central region of the caveolin-1 protein.
Le Lan
Charlotte
C
CEA Centre de Saclay, Département de Biologie Joliot-Curie and URA CNRS 2096, Service de Biophysique des Protéines et des Membranes, Bat 528, 91191 Gif sur Yvette Cedex, France.
Neumann
Jean-Michel
JM
Jamin
Nadège
N
D020816:Amino Acid Motifs; D051242:Caveolin 1 / Q000737:chemistry*; D002942:Circular Dichroism / Q000379:methods; D006801:Humans; D008567:Membranes, Artificial; D008823:Micelles; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D009842:Oligopeptides / Q000737:chemistry*; D010713:Phosphatidylcholines / Q000737:chemistry*; D010767:Phosphorylcholine / Q000031:analogs & derivatives* / Q000737:chemistry; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D051242:Caveolin 1; D008567:Membranes, Artificial; D008823:Micelles; D009842:Oligopeptides; D010713:Phosphatidylcholines; D010767:Phosphorylcholine; C028810:dodecylphosphocholine