Assessment of Key Amino-Acid Residues of CD36 in Specific Binding Interaction with an Oxidized Low-Density Lipoprotein

CD36 binds oxidized low-density lipoprotein (oxLDL). A synthetic peptide comprising amino-acid residues 149-168 of mouse CD36 was recently found to bind fluorescence-labeled oxLDL particles. Based on our oxLDL-binding analysis of various synthetic CD36 peptides, we suggest that not only hydrophilic...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2013, Vol.77 (5), p.1134-1137
Main Authors: TAKAI, Marie, TSUZUKI, Satoshi, MATSUNO, Yukari, KOZAI, Yuki, EGUCHI, Ai, MATSUMURA, Shigenobu, INOUE, Kazuo, FUSHIKI, Tohru
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biotin - metabolism
CD36
CD36 Antigens - chemistry
CD36 Antigens - metabolism
Humans
Hydrophobic and Hydrophilic Interactions
hydrophobic residues
Ligands
Lipoproteins, LDL - metabolism
Mice
Molecular Sequence Data
oxidized low-density lipoprotein/oxidized glycerophospholipids
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Protein Binding
specific binding
Substrate Specificity
synthetic peptides
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Summary:CD36 binds oxidized low-density lipoprotein (oxLDL). A synthetic peptide comprising amino-acid residues 149-168 of mouse CD36 was recently found to bind fluorescence-labeled oxLDL particles. Based on our oxLDL-binding analysis of various synthetic CD36 peptides, we suggest that not only hydrophilic residues (e.g., Lys164 and Lys166) but also hydrophobic ones (e.g., Phe153, Leu158, and Leu161) are critical to binding.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.130072