A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part II

Abstract

Human serum albumin (HSA) is the most abundant human plasma protein. HSA plays a crucial role in many binding endos- and exogenous substances, which affects their pharmacological effect. The innovative aspect of the study is not only the interaction of fatted (HSA) and defatted (dHSA) human serum albumin with ibuprofen (IBU), but the analysis of the influence of temperature on the structural modifications of albumin and the interaction between the drug and proteins from the temperature characteristic of near hypothermia (308 K) to the temperature reflecting inflammation in the body (312 K and 314 K). Ibuprofen is a non-steroidal anti-inflammatory drug. IBU is used to relieve acute pain, inflammation, and fever. To determine ibuprofen’s binding site in the tertiary structure of HSA and dHSA, fluorescence spectroscopy was used. On its basis, the fluorescent emissive spectra of albumin (5 × 10−6 mol/dm3) without and with the presence of ibuprofen (1 × 10−5–1 × 10−4 mol/dm3) was recorded. The IBU-HSA complex’s fluorescence was excited by radiation of wavelengths of λex 275 nm and λex 295 nm. Spectrophotometric spectroscopy allowed for recording the absorbance spectra (zero-order and second derivative absorption spectra) of HSA and dHSA under the influence of ibuprofen (1 × 10−4 mol/dm3). To characterize the changes of albumin structure the presence of IBU, circular dichroism was used. The data obtained show that the presence of fatty acids and human serum albumin temperature influences the strength and type of interaction between serum albumin and drug. Ibuprofen binds more strongly to defatted human serum albumin than to albumin in the presence of fatty acids. Additionally, stronger complexes are formed with increasing temperatures. The competitive binding of ibuprofen and fatty acids to albumin may influence the concentration of free drug fraction and thus its therapeutic effect.

A biophysical approach to study the impact of muscle relaxant drug tizanidine on stability and activity of serum albumins

“…Absorption spectra provide insight into information about the protein–ligand interactions. It also helps in understanding the effect of the ligand on the conformational change of the proteins 35,36 . Absorption spectroscopy helps in determining the quenching mechanism, whether static or dynamic.…”

“…It also helps in understanding the effect of the ligand on the conformational change of the proteins. 35,36 Absorption spectroscopy helps in determining the quenching mechanism, whether static or dynamic. In addition of ligand, shift in the wavelength of the absorption spectrum corresponds to the static mechanism; however, no change signifies the dynamic quenching.…”

Revisiting and Updating the Interaction between Human Serum Albumin and the Non-Steroidal Anti-Inflammatory Drugs Ketoprofen and Ketorolac

“…Steady-state fluorescence spectroscopy is one of the most used techniques to determine the quantitative binding parameters of different small compounds with proteins, including NSAIDs binding with albumin [48][49][50]. Figure 3A,B depict the steady-state fluorescence emission of HSA without and upon the successive additions of KTF and KTL, respectively.…”

Probing the Interaction between Isoflucypram Fungicides and Human Serum Albumin: Multiple Spectroscopic and Molecular Modeling Investigations

“…Each domain consists of two helical subdomains that are connected by random coils [12,13]. Due to its unique structural and biochemical properties, HSA plays a crucial role in various physiological processes, including the transport of endogenous and exogenous ligands [14,15]. HSA has been shown to interact with a wide range of small molecules, including drugs, metabolites, and environmental toxins such as insecticides and fungicides [16,17].…”