Analysis of human serum albumin (HSA) Conjugation with Gold Nanoparticles by UV-Vis Spectroscopy (CAT#: STEM-MB-0975-WXH)

Introduction

During the past decade, the development and application of nanomaterials have rapidly increased in different areas. Among these materials, gold nanoparticles (GNPs), due to their biocompatibility, optical characteristics, and surfaces that are easy to modify, was discovered as imaging agents and drug carriers in biology and medicine with extensive applications. A large number of molecules, ranging from drugs, siRNA, DNA, and proteins, with the addition of GNPs, have been widely applied in biomedicine, from in vitro biosensing to in vivo drug/gene delivery. Properties including size, shape, and surface chemistry are proven to govern GNP behavior in the body.
As the key extra cellular protein of the circulatory system, human serum albumin (HSA) results in approximately 60 percent of the total amount of plasma proteins with a 42 mg/mL concentration. HSA also supplies approximately 80 percent of the colloid osmotic pressure of blood. As a result, researchers consider plasma protein binding as one of the most critical physico chemical properties of exogenous compounds, particularly nanoparticles, which are capable of modifying their circulation, metabolism, elimination, as well as dynamics. Accordingly, it becomes relevant to study the binding energetic, conformations within the binding process of GNPs to HSA to reveal its binding mode in the body.