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Assessment of Binding Affinity between Drugs and Human Serum Albumin Using Nanoporous Anodic Alumina Photonic Crystals
journal contribution
posted on 2016-04-29, 00:00 authored by Mahdieh Nemati, Abel Santos, Cheryl Suwen Law, Dusan LosicIn
this study, we report an innovative approach aiming to assess
the binding affinity between drug molecules and human serum albumin
by combining nanoporous anodic alumina rugate filters (NAA-RFs) modified
with human serum albumin (HSA) and reflectometric interference spectroscopy
(RIfS). NAA-RFs are photonic crystal structures produced by sinusoidal
pulse anodization of aluminum that present two characteristic optical
parameters, the characteristic reflection peak (λPeak), and the effective optical thickness of the film (OTeff), which can be readily used as sensing parameters. A design of experiments
strategy and an ANOVA analysis are used to establish the effect of
the anodization parameters (i.e., anodization period and anodization
offset) on the sensitivity of HSA-modified NAA-RFs toward indomethacin,
a model drug. To this end, two sensing parameters are used, that is,
shifts in the characteristic reflection peak (ΔλPeak) and changes in the effective optical thickness of
the film (ΔOTeff). Subsequently, optimized NAA-RFs
are used as sensing platforms to determine the binding affinity between
a set of drugs (i.e., indomethacin, coumarin, sulfadymethoxine, warfarin,
and salicylic acid) and HSA molecules. Our results verify that the
combination of HSA-modified NAA-RFs with RIfS can be used as a portable,
low-cost, and simple system for establishing the binding affinity
between drugs and plasma proteins, which is a critical factor to develop
efficient medicines for treating a broad range of diseases and medical
conditions.