Spectroscopic approach of the interaction study of amphiphilic drugs with the serum albumins

Khan, Abbul Bashar; Khan, Javed Masood; Ali, Mushir; Khan, Rizwan Hasan; Din, Kabir-ud

doi:10.1016/j.colsurfb.2011.06.007

Cited by 40 publications

(22 citation statements)

References 41 publications

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“…Furthermore, the CD spectra of BSA/ HSA in the presence and absence of ergosterol were observed to be similar in shape, indicating that the structure of BSA/HSA was also predominantly a-helical even after binding to ergosterol [35].…”

Section: Ft-ir Spectra Analysismentioning

confidence: 88%

“…In order to examine the hydrophobic contact in the BSA-ergosterol and HSA-ergosterol complexes, the antisymmetric and symmetric CH 2 stretching vibrations of BSA/HSA [35] were investigated in the region 3,000-2,800 cm -1 . The CH 2 bands of free BSA located at 2961, 2932, and 2861 cm -1 shifted to 2970, 2946, and 2874 cm -1 (ergosterol), and the CH 2 bands of free HSA located at 2961, 2936, and 2873 cm -1 shifted to 2958, 2925, and 2854 cm -1 (ergosterol) in these protein-drug complexes (Fig.…”

Section: Hydrophobic Interactionsmentioning

confidence: 99%

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Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Cheng

2012

Mol Biol Rep

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This study was designed to examine the interactions of ergosterol with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions with the drug concentrations in the range of 2.99-105.88 μM and the concentration of proteins was fixed at 5.0 μM. The analysis of emission spectra quenching at different temperatures revealed that the quenching mechanism of HSA/BSA by ergosterol was the static quenching. The number of binding sites n and the binding constants K were obtained at various temperatures. The distance r between ergosterol and HSA/BSA was evaluated according to Föster non-radioactive energy transfer theory. The results of synchronous fluorescence, 3D fluorescence, FT-IR, CD and UV-Vis absorption spectra showed that the conformations of HSA/BSA altered in the presence of ergosterol. The thermodynamic parameters, free energy change (ΔG), enthalpy change (ΔH) and entropy change (ΔS) for BSA-ergosterol and HSA-ergosterol systems were calculated by the van't Hoff equation and discussed. Besides, with the aid of three site markers (for example, phenylbutazone, ibuprofen and digitoxin), we have reported that ergosterol primarily binds to the tryptophan residues of BSA/HSA within site I (subdomain II A).

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Section: Ft-ir Spectra Analysismentioning

confidence: 88%

Section: Hydrophobic Interactionsmentioning

confidence: 99%

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Cheng

2012

Mol Biol Rep

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“…In fact, the binding constants for imidazolium ionic liquids (ILs) and BSA are very low (in the order of 10 2 L mol −1 ) which indicate a very weak interaction between the ILs and the protein [58]. This situation clearly contrasts with the pyrrolidinium-based IL synthesized by Kumari et al [72] which showed K SV and K a values of 3.45 × 10 5 and 3.33 × 10 5 L mol −1 , respectively, in phosphate buffer (pH 7.4) at 298 K. Khan et al [65,70] studied the binding of amphiphilic drugs amitriptyline hydrochloride (AMT), promethazine hydrochloride (PMT), nortriptyline hydrochloride (NOT) and promazine hydrochloride (PMZ) with serum albumins HSA and BSA. Fluorescence quenching data for the drug-protein complexes yielded values of K SV = (2.51-5.28) × 10 4 L mol −1 , K a = (0.46-32.5) × 10 4 L mol −1 and G b values between −21.00 and −31.60 kJ mol −1 in Tris-HCl buffer solution (pH 7.4) at 310 K [65,70].…”

Section: Fluorescence Quenching Datamentioning

confidence: 61%

“…The K a values obtained for BSA-(C 12 Cys) 2 complexes suggest lower binding affinity compared to other strong protein-ligand complexes with binding constants ranging from 10 5 to 10 8 L mol −1 [71,72] However, lower binding constants (10 2 -10 4 L mol −1 ) have been reported for several other protein-ligand complexes [26,27,50,[65][66][67]70,73]. In fact, the binding constants for imidazolium ionic liquids (ILs) and BSA are very low (in the order of 10 2 L mol −1 ) which indicate a very weak interaction between the ILs and the protein [58].…”

Section: Fluorescence Quenching Datamentioning

confidence: 80%

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Amino acid-based cationic gemini surfactant–protein interactions

Branco

Pinheiro

Faustino

2015

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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The interaction between cepharanthine and two serum albumins: multiple spectroscopic and chemometric investigations

et al. 2013

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The binding modes of cepharanthine (CEPT) with bovine serum albumin (BSA) and human serum albumin (HSA) have been established by reproducing physiological conditions, which is very important to understand the pharmacokinetics and toxicity of CEPT. These spectral data were further analyzed by the multivariate curve resolution-alternating least squares method. Moreover, the concentration profiles and pure spectra of three species (BSA/HSA, CEPT and CEPT-BSA/HSA) and the apparent equilibrium constants K(app) were evaluated. The experimental results showed that CEPT could quench the fluorescence intensity of BSA/HSA by a combined quenching (static and dynamic) procedure. The binding constant (K), the thermodynamic parameters (ΔG, ΔH and ΔS) and binding subdomain were measured, and indicated that CEPT could spontaneously bind to BSA/HSA on subdomain IIA through the hydrophobic interactions. The effect of CEPT on the secondary structure of proteins has been analyzed by circular dichroism, 3D fluorescence and Fourier transform infrared spectra. The binding distance between CEPT and tryptophan of BSA/HSA was 2.305/1.749 nm, which is based on the Förster resonance energy transfer theory.

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Spectroscopic approach of the interaction study of amphiphilic drugs with the serum albumins

Cited by 40 publications

References 41 publications

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Amino acid-based cationic gemini surfactant–protein interactions

The interaction between cepharanthine and two serum albumins: multiple spectroscopic and chemometric investigations

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