Sterol affinity for phospholipid bilayers is influenced by hydrophobic matching between lipids and transmembrane peptides

• Published in: Biochimica et biophysica acta Vol. 1828; no. 3; pp. 932 - 937
• Main Authors: Ijäs, H. Kristian, Lönnfors, Max, Nyholm, Thomas K.M.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2013
• Subjects: 1,2-Dipalmitoylphosphatidylcholine - chemistry; beta-Cyclodextrins - chemistry; Biophysics - methods; Cholestenes - chemistry; Cholesterol; Dimyristoylphosphatidylcholine - chemistry; Dose-Response Relationship, Drug; Fluorescence spectroscopy; Hydrophobic and Hydrophilic Interactions; Kinetics; Lipid Bilayers - chemistry; Lipids - chemistry; Membrane trafficking; Model membrane; Models, Chemical; Models, Statistical; Peptides - chemistry; Phosphatidylcholines - chemistry; Phospholipids - chemistry; Protein sorting; Protein–lipid interaction; Sterols - chemistry; Fluorescence spectroscopy; KR; LUV; KX; Cholesterol; Model membrane; DPH-PC; mβCD; Membrane trafficking; Protein sorting; CTL; DLPC; DMPC; Protein–lipid interaction; DPPC

Lipid self-organization is believed to be essential for shaping the lateral structure of membranes, but it is becoming increasingly clear that also membrane proteins can be involved in the maintenance of membrane architecture. Cholesterol is thought to be important for the lateral organization of eu...