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Article

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

1
Faculty of Chemistry, University of Opole, Oleska 48, 45-052 Opole, Poland
2
Institute of Chemistry, University of Silesia in Katowice, Szkolna 9, 40-006 Katowice, Poland
*
Author to whom correspondence should be addressed.
Academic Editor: Helen D. Skaltsa
Sci. Pharm. 2021, 89(3), 30; https://doi.org/10.3390/scipharm89030030
Received: 30 April 2021 / Revised: 30 May 2021 / Accepted: 11 June 2021 / Published: 22 June 2021
(This article belongs to the Special Issue Feature Papers in Scientia Pharmaceutica)
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. View Full-Text
Keywords: human serum albumin; ibuprofen; spectrophotometric; spectrofluorometric; circular dichroism human serum albumin; ibuprofen; spectrophotometric; spectrofluorometric; circular dichroism
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MDPI and ACS Style

Ploch-Jankowska, A.; Pentak, D.; Nycz, J.E. A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part II. Sci. Pharm. 2021, 89, 30. https://doi.org/10.3390/scipharm89030030

AMA Style

Ploch-Jankowska A, Pentak D, Nycz JE. A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part II. Scientia Pharmaceutica. 2021; 89(3):30. https://doi.org/10.3390/scipharm89030030

Chicago/Turabian Style

Ploch-Jankowska, Anna, Danuta Pentak, and Jacek E. Nycz 2021. "A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part II" Scientia Pharmaceutica 89, no. 3: 30. https://doi.org/10.3390/scipharm89030030

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