Recent Advances in using the Quartz Crystal Microbalance to Analyze the Binding of Drug Ligands to Serum Albumin Proteins

Abstract

There has been a dearth in understanding
how interactions between drug molecules
and macromolecules can inform rational
drug design [1]. Understanding the
thermodynamic, structural, and kinetic aspects
of these interactions are key to progressing the
development of novel drugs. Many of these
studies utilize either bovine serum albumin
(BSA) or human serum albumin (HSA) as
their drug target [2-7]. BSA is a standard serum
albumin protein that functions as a transporter
of drugs [8]. HSA is a serum albumin protein
found within human blood that functions as
a transporter of various compounds, acts as
an antioxidant, and plays important roles in
drug delivery [2]. The use of these two serum
albumin proteins in drug binding studies has
led to a better understanding of the interaction
between drug molecules and albumin [3,4].
Studies using HSA are particularly attractive
to the pharmaceutical industry because of
its ability to bind a myriad of drugs, giving
insight into the drug’s delivery and efficacy,
while decreasing side effects of these drugs
[5].