A comparative study of the interaction of Tamiflu and Oseltamivir carboxylate with bovine serum albumin

Vishkaee, Tahereh Sadigh; Mohajerani, Niloufar; Nafisi, Shohreh

doi:10.1016/j.jphotobiol.2012.11.003

Cited by 5 publications

(3 citation statements)

References 41 publications

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“…For small chemical drugs, Δ G can be calculated from the binding constant ( K B ) according to the equation Δ G = − RT ln K B . The values of Δ G of binding for small molecule drugs and BSA range from −29.2 to −21 kJ/mol − (detailed data in Table S1, Supporting Information), much more positive than that between IFN and BSA (−92.8 ± 5.8 kJ/mol).…”

Section: Resultsmentioning

confidence: 99%

Modeling the Interaction of Interferon α-1b to Bovine Serum Albumin as a Drug Delivery System

et al. 2014

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Protein-based nanoparticles represent a promising approach to carry polypeptide and protein drugs. Using both theory and experimentation, an interferon α-1b (IFN) delivery system carried by bovine serum albumin (BSA) nanoparticles was designed. Theoretical results indicate the most probable binding site and interaction mechanism for IFN on BSA. IFN has a higher binding affinity with BSA compared with small chemical drugs. The drug loading is about 8 mg/g, significantly higher than those reported in other literature. The release profiles differ between the nanoparticles prepared by the incorporation method and the adsorption method. The adsorption of IFN on BSA nanoparticles is monolayer adsorption. The fact that IFN was carried successfully by BSA nanoparticles establishes a solid basis for expanding the drug loading field of BSA nanoparticles to proteins and polypeptides.

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Section: Resultsmentioning

confidence: 99%

Modeling the Interaction of Interferon α-1b to Bovine Serum Albumin as a Drug Delivery System

et al. 2014

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“…Chemically, Oseltamivir is a synthetic cyclohexenecarboxylate ester with antiviral activity whose IUPAC name is ethyl (3R,4R,5S)-4-acetamido-5-amino-3-pentan-3-yloxycyclohexene-1-carboxylate [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19]. Oseltamivir is used in health sciences for the treatment of influenza A and influenza B [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Behaviours of antiviral Oseltamivir in different media: DFT and SQMFF calculations

et al. 2021

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“…Serum albumins are one of the major soluble protein components present in the circulatory system that perform numerous physiological functions, including regulation of osmotic pressure, maintenance of blood pH, and distribution and transportation of various endogenous and exogenous molecules such as drugs, food additives, etc. − The approximate concentration of serum albumin in human blood is 3.6–5.2 g/dL, which can be increased up to double . The drug or ligand molecule binds with albumin either weakly or strongly.…”

Section: Introductionmentioning

confidence: 99%

Privileged Scaffold Chalcone: Synthesis, Characterization and Its Mechanistic Interaction Studies with BSA Employing Spectroscopic and Chemoinformatics Approaches

et al. 2020

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Chalcone, a privileged structure, is considered as an effective template in the field of medicinal chemistry for potent drug discovery. In the present study, a privileged template chalcone was designed, synthesized, and characterized by various spectroscopic techniques (NMR, high-resolution mass spectrometry, Fourier transform infrared (FT-IR) spectroscopy, UV spectroscopy, and single-crystal X-ray diffraction). The mechanism of binding of chalcone with bovine serum albumin (BSA) was determined by multispectroscopic techniques and computational methods. Steady-state fluorescence spectroscopy suggests that the intrinsic fluorescence of BSA was quenched upon the addition of chalcone by the combined dynamic and static quenching mechanism. Time-resolved spectroscopy confirms complex formation. FT-IR and circular dichroism spectroscopy suggested the presence of chalcone in the BSA molecule microenvironment and also the possibility of rearrangement of the native structure of BSA. Moreover, molecular docking studies confirm the moderate binding of chalcone with BSA and the molecular dynamics simulation analysis shows the stability of the BSA−drug complex system with minimal deformability fluctuations and potential interaction by the covariance matrix. Moreover, pharmacodynamics and pharmacological analysis show good results through Lipinski rules, with no toxicity profile and high gastrointestinal absorptions by boiled egg permeation assays. This study elucidates the mechanistic profile of the privileged chalcone scaffold to be used in therapeutic applications.

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A comparative study of the interaction of Tamiflu and Oseltamivir carboxylate with bovine serum albumin

Cited by 5 publications

References 41 publications

Modeling the Interaction of Interferon α-1b to Bovine Serum Albumin as a Drug Delivery System

Modeling the Interaction of Interferon α-1b to Bovine Serum Albumin as a Drug Delivery System

Behaviours of antiviral Oseltamivir in different media: DFT and SQMFF calculations

Privileged Scaffold Chalcone: Synthesis, Characterization and Its Mechanistic Interaction Studies with BSA Employing Spectroscopic and Chemoinformatics Approaches

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