This study uses label-free methods to determine the binding interactions of lysophosphatidic acid (LPA) with bovine and human serum albumin (BSA and HSA). LPA is a bioactive lysophospholipid (LysoPL) Show more
This study uses label-free methods to determine the binding interactions of lysophosphatidic acid (LPA) with bovine and human serum albumin (BSA and HSA). LPA is a bioactive lysophospholipid (LysoPL) that signals through a G-protein-coupled receptor (GPCR). Plasma LPAs are primarily carried by albumin; however, their binding interactions with the carrier protein (HSA) are not as well studied as those with fatty acids, drugs, or metal ions. Therefore, the aim of this study is to determine the binding sites of LPA in serum albumin through spectroscopic methods. Intrinsic fluorescence quenching experiments in conjunction with a label-free, free solution light interferometric assay have been employed to determine the binding Show less