Abstract 1252 Decoupling Specific from Non-Specific Binding Mechanisms of 8-Anilinonaphthalene-1-Sulfonic Acid and Epigallocatechin Gallate Ligands to the Bovine Serum Albumin Protein

In this study, quartz crystal microbalance (QCM) and fluorimeter experiments were combined to decouple specific and non-specific binding of two ligands on the serum albumin protein. Serum albumin is the most abundant protein in the bloodstream and is a hydrophobic carrier for delivering ligands to cells. The ligand 8-anilinonaphthalene-1-sulfonic acid (ANS) is known to have a high affinity for serum albumin, and fluoresces when complexed with the protein. The ligand epigallocatechin gallate (EGCG) is a polyphenol in green tea known for its antioxidant properties, and is approximately 1.5 times heavier than ANS.