Interaction study of pioglitazone with albumin by fluorescence spectroscopy and molecular docking

Faridbod, Farnoush; Ganjali, Mohammad Reza; Larijani, Bagher; Riahi, Siavash; Saboury, Ali Akbar; Hosseini, Morteza; Norouzi, Parviz; Pillip, Christoph

doi:10.1016/j.saa.2010.09.001

Cited by 81 publications

(35 citation statements)

References 21 publications

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“…However, as stated earlier, adsorption, distribution, metabolism and elimination (ADME) is controlled by albumin [40]. Poor or strong binding to HSA is believed to affect half-time of drugs [41], and their dosage depends on their half-life in plasma. Thus, the binding affinity of any drug to HSA is one of the major factors that determine the pharmacokinetics, halftime, and availability of the drug in various tissues [40].…”

Section: Discussionmentioning

confidence: 98%

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Yasmeen

Riyazuddeen

Rabbani

2016

J Therm Anal Calorim

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Amoxicillin is a common antibiotic drug used for preventing bacterial colonization of urinary and skin infections. The binding of amoxicillin (AX) to human serum albumin (HSA) in sodium phosphate buffer solution at pH 7.4 has been investigated by UV-visible spectroscopy, fluorescence spectroscopy, Förster resonance energy transfer, isothermal titration calorimetry (ITC), circular dichroism (CD) and FTIR spectroscopy. The binding studies using ITC revealed that the interaction is entropy driven rather than enthalpy as the change in enthalpy (DH°) and change in entropy (TDS°) both are positive, indicating the endothermic reaction with low affinity and hydrophobic interaction. UV-visible absorption spectra of HSA are increased upon addition of AX which shows complex formation of HSA-AX. The fluorescence spectra reveal that the AX has an ability to quench the intrinsic fluorescence of HSA tryptophan through a static quenching procedure. The molecular distance r between donor (HSA) and acceptor (AX) was estimated according to Förster theory of nonradiative energy transfer. The CD spectra showed that the a-helix of HSA increases with increasing the amount of AX. The thermal denaturation has been studied by far-UV CD, and it is found that HSA stability is decreased by the complex formation of HSA and AX. The remarkable change in amide I peak position in infrared spectrum after interaction with AX indicated that secondary structure of HSA has been changed.

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Section: Discussionmentioning

confidence: 98%

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Yasmeen

Riyazuddeen

Rabbani

2016

J Therm Anal Calorim

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“…Poor or strong binding to PA or infused PGA is believed to affect half-time of drugs [36], and their dosage depends on their half-life/bioavailability in plasma.…”

Section: Resultsmentioning

confidence: 99%

Comparative studies on drug binding to the purified and pharmaceutical-grade human serum albumins: Bridging between basic research and clinical applications of albumin

et al. 2015

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“…The ligand-binding characteristics of HSA have been extensively reviewed (5,6) while many techniques have been utilized to study the protein binding interactions. To name some of them: X-ray diffraction (7), fluorescence spectroscopy (8), circular dichroism spectroscopy (9), high-performance affinity chromatography (10), and equilibrium dialysis (11).…”

Section: Introductionmentioning

confidence: 99%

Assessment of the Dissociation Energetics of Some Selected Ligand Drugs Bound on Human Serum Albumin by Differential Scanning Calorimetry

Faroongsarng

2015

AAPS PharmSciTech

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Abstract. Drug-protein binding may play a role in the thermal energetics of protein denaturation and could lead to the determination of its equilibrium dissociation parameter. The aim of this study was to assess the energetics of a drug that was bound to human serum albumin (HSA) during thermal denaturation. Drugs that were bound at a single high-affinity primary binding site on HSA, including diazepam and ibuprofen, were employed. Commercial HSA was treated with charcoal to remove stabilizers and adjusted to 20% w/v in a pH 7.4 buffered solution. Serial concentrations of individual drugs up to 0.16 mmole/g-protein were added to the cleaned HSA solutions whereas diazepam was added to a commercial HSA solution. Samples were subjected to differential scanning calorimetry (DSC) set to run from 37 to 90°C at 3.0°C/min. Binding of the drug slightly increased the denaturing temperature of the cleaned HSA due to a shift in the equilibrium toward the native protein bound with the drug. Diazepam depressed the denaturing temperature of the commercial HSA by competing with the stabilizers already bound to the primary site of the HSA. This yielded not only the HSA-stabilizer but also the HSAdiazepam type complexes that exhibited a different denaturation process. A rational approximation of the Lumry-Eyring protein denaturation model was used to treat the DSC endotherms. The approximated scheme: N → k 3 K P was successfully fitted to the data. It was used to determine the dissociation parameters for diazepam and ibuprofen bound to the HSA. These results were comparable to those obtained from other methods.

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Interaction study of pioglitazone with albumin by fluorescence spectroscopy and molecular docking

Cited by 81 publications

References 21 publications

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Calorimetric and spectroscopic binding studies of amoxicillin with human serum albumin

Comparative studies on drug binding to the purified and pharmaceutical-grade human serum albumins: Bridging between basic research and clinical applications of albumin

Assessment of the Dissociation Energetics of Some Selected Ligand Drugs Bound on Human Serum Albumin by Differential Scanning Calorimetry

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