Reference : Structure and orientation of apo B-100 peptides into a lipid bilayer.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/65875
Structure and orientation of apo B-100 peptides into a lipid bilayer.
English
Lins, Laurence mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Brasseur, Robert mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Rosseneu, M. [> > > >]
Yang, C. Y. [> > > >]
Sparrow, D. A. [> > > >]
Sparrow, J. T. [> > > >]
Gotto, A M Jr [> > > >]
Ruysschaert, J. M. [> > > >]
1994
Journal of Protein Chemistry
Kluwer Academic/Plenum Publishers
13
1
77-88
Yes (verified by ORBi)
International
0277-8033
New York
NY
[en] Apolipoprotein B-100 ; Apolipoproteins B/chemistry ; Binding Sites ; Dimyristoylphosphatidylcholine ; Indicators and Reagents ; Lipid Bilayers ; Peptide Fragments/chemical synthesis/chemistry ; Protein Structure, Secondary ; Spectroscopy, Fourier Transform Infrared/methods
[en] Peptides corresponding to lipid binding domains of Apo B-100 were synthesized, purified, and incubated with dimyristoylphosphatidylcholine (DMPC) liposomes. The secondary structure of the apo B-100 peptide-lipid complexes was evaluated by attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Those peptides belonging to the hydrophobic "core" domain of apo B-100 when associated with phospholipids were rich in beta sheet structure; a predominant alpha helical conformation was shown to be associated with one peptide located in a surface region of apo B-100. IR dichroic spectra revealed, in the case of the "core" peptides, that the beta sheet component is the only oriented structure with respect to the phospholipid acyl chains. This orientation of the beta sheet was recently found in LDL particles after proteolytic digestion by trypsin (Goormaghtigh, E., Cabiaux, V., De Meutter, J., Rosseneu, M., and Ruysschaert, J. M., 1993, Biochemistry 32, 6104-6110). Altogether, the data suggest that beta sheet, present in a high proportion in the native apo B-100, is probably another protein structure in addition to the amphipathic helix which strongly interacts with the lipid outer layer surrounding the LDL particle.
Researchers ; Professionals
http://hdl.handle.net/2268/65875

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