Molecular mechanism and thermodynamic study of Rosuvastatin interaction with human serum albumin using a surface plasmon resonance method combined with a multi-spectroscopic, and molecular modeling approach

Afkham, Sheida; Hanaee, Jalal; Zakariazadeh, Mostafa; Fathi, Farzaneh; Shafiee, Samira; Soltani, Somaieh

doi:10.1016/j.ejps.2021.106005

Cited by 13 publications

(21 citation statements)

References 27 publications

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“…Generally, aromatic carboxylic acids with a peripheric negative charge, that is distantly located from the hydrophobic centre, are lodged in the FA4 site [30]. Our data are in agreement with previous biochemical studies reporting that the majority of contraindicated drugs knowns to have adverse effects when co-administered with GEM appear to bind either or both Sudlow's binding sites I and II [36][37][38][39][40]. Overall, the protein complex HSA-GEM was superimposed well with that of other well-known HSA-drug binding complexes examined here.…”

Section: Discussionsupporting

confidence: 92%

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Liberi

Linciano

Moro

et al. 2022

IJMS

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Gemfibrozil (GEM) is an orally administered lipid-regulating fibrate derivative drug sold under the brand name Lopid®, among others. Since its approval in the early 80s, GEM has been largely applied to treat hypertriglyceridemia and other disorders of lipid metabolism. Though generally well tolerated, GEM can alter the distribution and the free, active concentration of some co-administered drugs, leading to adverse effects. Most of them appear to be related to the ability of GEM to bind with high affinity human serum albumin (HSA), the major drug-carrier protein in blood plasma. Here, we report the crystal structure of HSA in complex with GEM. Two binding sites have been identified, namely Sudlow’s binding sites I (FA7) and II (FA3–FA4). A comparison of the crystal structure of HSA in complex with GEM with those of other previously described HSA–drug complexes enabled us to appreciate the analogies and differences in their respective binding modes. The elucidation of the molecular interaction between GEM and HSA might offer the basis for the development of novel GEM derivatives that can be safely and synergistically co-administered with other drugs, enabling augmented therapeutic efficacies.

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Section: Discussionsupporting

confidence: 92%

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Liberi

Linciano

Moro

et al. 2022

IJMS

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“…The linear relationship between F 0 / F and [ Q ] confirmed that there was only one type of quenching, either dynamic or static. The values of K SV decrease as the temperature rises from 303 K to 323 K to 338 K, which is suggestive of static quenching, [ 26–28 ] as shown in Figure 5c.…”

Section: Resultsmentioning

confidence: 92%

Utility of a xanthene‐based dye for determination of nilotinib using two spectroscopic approaches. Applications to bulk powder, capsules, and spiked human plasma

et al. 2023

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Novel, selective, facile, and precise spectroscopic approaches were validated to determine nilotinib hydrochloride, a tyrosine kinase inhibitor used to treat patients with chronic myeloid leukemia. These approaches depend on the reaction of the tertiary amine group of nilotinib with erythrosine B in the Britton-Robinson buffer at pH 4.Method I, depends on measuring the absorbance of the formed complex at 551 nm.The absorbance concentration plot showed linearity over the concentration range of 1.0 to 9.0 μg/ml. Method II, involved the measurement of the quenching of the native fluorescence of erythrosine B by adding nilotinib in an acidic medium. The fluorescence quenching of erythrosine B was measured at 549 nm after excitation at 528 nm. This approach showed excellent linearity in the concentration range of 0.04 to 0.7 μg/ml. The limit of detection values for Method I and Method II were 0.225 and 0.008 μg/ml, respectively, while the limit of quantitation values for Method I and Method II were 0.68 and 0.026 μg/ml, respectively. To get the optimal conditions, factors that may affect the formation of the ion-pairing complex were thoroughly examined. The two approaches were carefully validated following the International Conference of Harmonization (ICH Q2R1) guidelines. Statistical assessment of the results achieved using the suggested and previously published comparison approaches showed no significant difference. The approaches were successful in determining nilotinib in a pharmaceutical dosage form as well as spiked human plasma samples. The eco-friendly properties of the methods were evaluated by three different tools.

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“…4c shows an increase in K sv values from 8.8 × 10 3 to 17.2 × 10 3 L mol −1 with an increase in temperature from 303 to 323 K, indicating dynamic quenching. 31–33…”

Section: Resultsmentioning

confidence: 99%

“…Additionally, the bimolecular quenching constant ( K q ) could be calculated from the following equation: 33 where τ o is the lifetime of native radiation of AC (5 × 10 −9 s); therefore, the calculated values of K q were 1.76 × 10 12 and 3.44 × 10 12 L mol −1 s −1 within a temperature range of 303–323 K. Moreover, the calculation of the binding site number and rate constant of the reaction between AC and TR was performed according to the modified Stern–Volmer plot (Fig. 4d) from the following equation: 34,35 where K b is the reaction rate constant, n is the number of binding sites, [ D ] is the molar concentration of TR, and F 0 and F are the fluorescence intensities of AC in the absence and presence of TR, respectively.…”

Section: Resultsmentioning

confidence: 99%

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Utility of a novel turn-off fluorescence probe for the determination of tranilast, an adjunctive drug for patients with severe COVID-19

et al. 2022

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Molecular mechanism and thermodynamic study of Rosuvastatin interaction with human serum albumin using a surface plasmon resonance method combined with a multi-spectroscopic, and molecular modeling approach

Cited by 13 publications

References 27 publications

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil

Utility of a xanthene‐based dye for determination of nilotinib using two spectroscopic approaches. Applications to bulk powder, capsules, and spiked human plasma

Utility of a novel turn-off fluorescence probe for the determination of tranilast, an adjunctive drug for patients with severe COVID-19

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