Description:
<jats:p>Lysophosphatidylcholine, a major phospholipid component of oxidized low‐density lipoprotein, is implicated in many inflammatory diseases, including atherosclerosis. We previously reported that Asp‐hemolysin‐related synthetic peptide (P21) composed of 21 amino acid residues markedly inhibits the bioactivities of oxidized low‐density lipoprotein and lysophosphatidylcholine, by directly binding to oxidized low‐density lipoprotein and lysophosphatidylcholine. Here, to clarify whether P21 specifically binds to lysophosphatidylcholine and what forms of lysophosphatidylcholine with which P21 interact, we investigated the interaction between P21 containing two tryptophan residues and lysophosphatidylcholine by using fluorescence spectroscopy, polyacrylamide gel electrophoresis, and surface plasmon resonance. From tryptophan fluorescence measurements, N‐terminally biotinylated P21 specifically interacted with lysophosphatidylcholine, at concentrations exceeding the critical micelle concentration. From tryptophan fluorescence quenching, the tryptophan residues in biotinylated P21 in the presence of lysophosphatidylcholine were mostly exposed on the outer side of the peptide. From polyacrylamide gel electrophoresis and surface plasmon resonance, bound to 1‐palmitoyl‐lysophosphatidylcholine at concentrations higher than 100 μ<jats:sc>m</jats:sc>, ensuring stable micelles. These results indicate that biotinylated P21 specifically recognizes lysophosphatidylcholine micelles. Further study of the interaction between biotinylated P21 and lysophosphatidylcholine micelles may provide important information for the prevention and treatment for many inflammatory diseases caused by lysophosphatidylcholine micelles.</jats:p>