In vitro Analysis of the Interaction between Ketorolac Tromethamine and Bovine Serum Albumin Using Fluorescence Spectroscopy

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

“…These drugs bind with HSA to be distributed in the bloodstream, particularly impacting the desired therapeutic effects (pharmacokinetic and pharmacodynamic effects) [7]. The biophysical characterization of the interaction between albumin and the NSAIDs, more specifically KTF and KTL, was primarily determined by other authors via spectroscopy without considering some pitfalls, e.g., the inner filter correction and the use of different mathematical approximations without considering the fluorescence quenching mechanisms [28][29][30][31]. Thus, we revised and updated the biophysical characterizations of HSA:KTF and HSA:KTL via multiple spectroscopic techniques combined with molecular docking.…”

“…Hence, Figure 4A,B depict the decays The number of binding sites (n) related to the association of HSA:NSAIDs is close to 1 (Table 1), indicating that the HSA protein interacts with one drug molecule [53]. The binding constant (K b ) values are in the range of 10 4 -10 5 M −1 for HSA:KTF and in the order of 10 4 M −1 for HSA:KTL, indicating moderate binding affinity [27][28][29][30][31][32]. The thermodynamics parameters of the HSA:KTF and HSA:KTL interaction were also determined, and the results are summarized in Table 1.…”

“…In this case, they identified the subdomain IIA (site II) as the main binding site for IBU, which was subsequently confirmed by X-ray crystallographic data [23], and for this reason, this NSAID is widely used as a site marker in drug-displacement assays with albumin [24,25]. Recently, there have been different reports about the determination of the thermodynamic parameters and binding affinity between albumin and NSAIDs by multiple spectroscopic techniques with different mathematical approaches, e.g., double logarithmic approximation, the Stern-Volmer equation, the modified Stern-Volmer equation, and the Klotz model [26][27][28][29][30][31][32]. Unfortunately, most approaches do not consider inner filter correction in the steady-state fluorescence data and do not recognize the main fluorescence quenching mechanism using reliable instrumental methods.…”

“…Ketoprofen (KTF) and ketorolac (KTL) are among the most used NSAIDs in humans to alleviate moderate pain and to treat some diseases, e.g., rheumatoid arthritis, osteo-arthritis, and dysmenorrhea [33][34][35][36]. However, their binding affinity with albumin was primarily determined by spectroscopy without considering the pitfalls raised above [28][29][30][31]. Thus, the present work aims to update the determination of the binding affinities of HSA:KTF and HSA:KTL by using the 1 H saturation-transfer difference nuclear magnetic resonance ( 1 H STD-NMR), ultraviolet (UV) absorption, circular dichroism (CD), steady-state, and time-resolved fluorescence techniques combined with in silico calculations.…”

Smart Spectrophotometric Methods Based on Feasible Mathematical Processing and Classical Chemometry for The Simultaneous Assay of Alcaftadine and Ketorolac in Their Recently Approved Pharmaceutical Formulation.

“…2) [9]. Different methods have been reported for the assay of ALC and KET, including Spectrophotometric [4,7,[10][11][12][13][14][15], LC-MS [6], HPLC [7,[16][17][18][19][20], HPTLC [21][22][23][24], fluorescence [25,26] and electrochemical methods [27,28]. Derivative spectrophotometry (DS) is a sophisticated modern method.…”