Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers.
We report an X-ray reflectivity study on the effects of adsorption of myelin basic protein (MBP) on Langmuir monolayers and on deposited Langmuir-Schaefer multilayers of the phospholipid dipalmitoyl phosphatidylglycerol (DPPG). We provide for the first time, direct microscopic evidence on the destructuring effects of MBP leading to plasticity of the DPPG layers supporting commonly accepted models of the stabilizing role of MBP in the myelin membrane. We also show how protein adsorption onto the layer is determined both by electrostatic and nonspecific hydrophobic interactions.
Cristofolini
L
L
Dipartmento di Fisica e Istituto Nazionale per la Fisica della Materia, Universita' di Parma, Parco Area delle Scienze 7a, 43100 Parma, Italy. cristofolini@fis.unipr.it
Fontana
M P
MP
Serra
F
F
Fasano
A
A
Riccio
P
P
Konovalov
O
O
D000327:Adsorption; D003198:Computer Simulation; D008051:Lipid Bilayers / Q000737:chemistry*; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D004676:Myelin Basic Protein / Q000737:chemistry*; D044367:Phase Transition; D010743:Phospholipids / Q000737:chemistry*; D011485:Protein Binding
D008051:Lipid Bilayers; D008565:Membrane Proteins; D004676:Myelin Basic Protein; D010743:Phospholipids