Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Notes
Assessment of Key Amino-Acid Residues of CD36 in Specific Binding Interaction with an Oxidized Low-Density Lipoprotein
Marie TAKAISatoshi TSUZUKIYukari MATSUNOYuki KOZAIAi EGUCHIShigenobu MATSUMURAKazuo INOUETohru FUSHIKI
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2013 Volume 77 Issue 5 Pages 1134-1137

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Abstract
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.
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© 2013 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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