Structure and orientation of apo B-100 peptides into a lipid bilayer.
Structure and orientation of apo B-100 peptides into a lipid bilayer.
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apo B-100 肽进入脂质双层的结构和方向。
DOI：
10.1007/bf01891995
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
Ruysschaert,JM
中科院分区：
文献类型：
--
作者：
Lins,L;Brasseur,R;Rosseneu,M;Yang,CY;Sparrow,DA;Sparrow,JT;GottoJr,AM;Ruysschaert,JM
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 inΒsheet structure; a predominantαhelical 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 theΒsheet component is the only oriented structure with respect to the phospholipid acyl chains. This orientation of theΒsheet 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,Biochemistry32, 6104–6110). Altogether, the data suggest thatΒsheet, 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.
