Investigation of ketoprofen binding to human serum albumin by spectral methods

Bi, Shuyun; Yan, Lili; Sun, Ya‐Guang; Zhang, Hanqi

doi:10.1016/j.saa.2010.11.002

Cited by 52 publications

(47 citation statements)

References 23 publications

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“…The first system under study is that of the KET-BSA interaction. This interaction is of physiological significance because KET is a widely prescribed NSAID, which is transported in plasma via its interaction with HSA, the human analog of BSA (Bi et al, 2010). BSA is a 67 kDa monomer with an estimated τ c ~40 nsec and the K d of its interaction with KET is ~0.3 μM (Sowell et al, 2001).…”

Section: Resultsmentioning

confidence: 99%

Comparison of the sensitivities of WaterLOGSY and saturation transfer difference NMR experiments

2014

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The WaterLOGSY (WL) and Saturation Transfer Difference (STD) NMR experiments have proven to be extremely useful techniques to characterize interactions between small molecules and large biomolecules. In this work we compare the relative sensitivities of WL and STD NMR using 3 experimental systems: ketoprofen (KET)-bovine serum albumin (BSA), tert-butyl hydroquinone (TBHQ)-hemagglutinin (HA), and chloramphenicol (CAM)-ribosome (70S). In all cases we find that WL is more sensitive than STD for a given experimental time with the ratios ranging from 3.2 for KET-BSA to 16 for TBHQ-HA and CAM-70S. We attribute the increased sensitivity of WL to be due to simultaneous saturation of multiple sources of cross correlation, including direct NOEs of 1H of water and exchangeable groups and indirect NOEs of 1H-C groups. We suggest that the outstanding sensitivity of WL make it ideally suited for drug screening efforts targeting very large biomolecules at relatively low concentrations.

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Section: Resultsmentioning

confidence: 99%

Comparison of the sensitivities of WaterLOGSY and saturation transfer difference NMR experiments

2014

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“…From Table 2, it appears that the K values decreased with increasing the temperature, which exhibits that the quenching mechanism is a static quenching [20]. The DG1 of negative sign shows that the interactions between MC540 and FL are spontaneous processes.…”

Section: Determination Of Binding Parametersmentioning

confidence: 88%

Fluorescence quenching of fluorescein by Merocyanine 540 in liposomes

Toprak

Aydın

Arık

et al. 2011

Journal of Luminescence

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“…The affinity of albumin for copper was also determined by fluorescence. This method is based on the quenching of albumin fluorescence induced by its interaction with metal [37]. The intrinsic fluorescence of bovine albumin is mainly attributed to the tryptophan residues.…”

Section: Copper Binding Affinities Of Albuminmentioning

confidence: 99%

Deciphering metal-induced oxidative damages on glycated albumin structure and function

Baraka-Vidot¹,

Navarra

Leone

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background: Metal ions such as copper or zinc are involved in the development of neurodegenerative pathologies and metabolic diseases such as diabetes mellitus. Albumin structure and functions are impaired following metaland glucose-mediated oxidative alterations. The aim of this study was to elucidate effects of Cu(II) and Zn(II) ions on glucose-induced modifications in albumin by focusing on glycation, aggregation, oxidation and functional aspects. Methods: Aggregation and conformational changes in albumin were monitored by spectroscopy, fluorescence and microscopy techniques. Biochemical assays such as carbonyl, thiol groups, albumin-bound Cu, fructosamine and amine group measurements were used. Cellular assays were used to gain functional information concerning antioxidant activity of oxidized albumins. Results: Both metals promoted inhibition of albumin glycation associated with an enhanced aggregation and oxidation process. Metal ions gave rise to the formation of β-amyloid type aggregates in albumin exhibiting impaired antioxidant properties and toxic activity to murine microglia cells (BV2). The differential efficiency of both metal ions to inhibit albumin glycation, to promote aggregation and to affect cellular physiology is compared. Conclusions and general significance: Considering the key role of oxidized protein in pathology complications, glycation-mediated and metal ion-induced impairment of albumin properties might be important parameters to be followed and fought.

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Investigation of ketoprofen binding to human serum albumin by spectral methods

Cited by 52 publications

References 23 publications

Comparison of the sensitivities of WaterLOGSY and saturation transfer difference NMR experiments

Comparison of the sensitivities of WaterLOGSY and saturation transfer difference NMR experiments

Fluorescence quenching of fluorescein by Merocyanine 540 in liposomes

Deciphering metal-induced oxidative damages on glycated albumin structure and function

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