Electrochemical site marker competitive method for probing the binding site and binding mode between bovine serum albumin and alizarin red S

2011 ◽  
Vol 56 (11) ◽  
pp. 4181-4187 ◽  
Author(s):  
Hai Wu ◽  
Xiaojuan Zhao ◽  
Po Wang ◽  
Zong Dai ◽  
Xiaoyong Zou
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Binding Mode ◽  
Alizarin Red S ◽  
Alizarin Red ◽  
Site Marker

Effects of Cu2+ and pH on the binding of alizarin red S to bovine serum albumin based on the analysis of protein conformation

2014 ◽  
Vol 6 (13) ◽  
pp. 4729-4733 ◽  
Author(s):  
Hai Wu ◽  
Suhua Fan ◽  
Hong Chen ◽  
Jie Shen ◽  
Yanyan Geng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Analysis ◽  
Protein Conformation ◽  
Bovine Serum ◽  
Alizarin Red S ◽  
Alizarin Red

Effects of Cu2+ and pH on the interaction between alizarin red S and bovine serum albumin based on conformational analysis.

Investigation of Optical Spectroscopic and Computational Binding Mode of Bovine Serum Albumin with 1, 4-Bis ((4-((4-Heptylpiperazin-1-yl) Methyl)-1H-1, 2, 3-Triazol-1-yl) Methyl) Benzene

2015 ◽  
Vol 29 (8) ◽  
pp. 373-381 ◽  
Author(s):  
Subramani Karthikeyan ◽  
Shanmugavel Chinnathambi ◽  
Ayyavoo Kannan ◽  
Perumal Rajakumar ◽  
Devadasan Velmurugan ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Mode ◽  
Methyl Benzene

scholarly journals Ketoprofen-Based Ionic Liquids: Synthesis and Interactions with Bovine Serum Albumin

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 90 ◽  
Author(s):  
Paula Ossowicz ◽  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Joanna Klebeko ◽  
Ewelina Świątek ◽  
...  
Keyword(s):  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Binding Mode ◽  
Pharmaceutical Ingredients ◽  
System A ◽  
Static Mechanism

The development of ionic liquids based on active pharmaceutical ingredients (API-ILs) is a possible solution to some of the problems of solid and/or hydrophobic drugs such as low solubility and bioavailability, polymorphism and an alternative route of administration could be suggested as compared to the classical drug. Here, we report for the first time the synthesis and detailed characterization of a series of ILs containing a cation amino acid esters and anion ketoprofen (KETO-ILs). The affinity and the binding mode of the KETO-ILs to bovine serum albumin (BSA) were assessed using fluorescence spectroscopy. All compounds bind in a distance not longer than 6.14 nm to the BSA fluorophores. The estimated binding constants (KA) are in order of 105 L mol−1, which is indicative of strong drug or IL-BSA interactions. With respect to the ketoprofen-BSA system, a stronger affinity of the ILs containing l-LeuOEt, l-ValOBu, and l-ValOEt cation towards BSA is clearly seen. Fourier transformed infrared spectroscopy experiments have shown that all studied compounds induced a rearrangement of the protein molecule upon binding, which is consistent with the suggested static mechanism of BSA fluorescence quenching and formation of complexes between BSA and the drugs. All tested compounds were safe for macrophages.

scholarly journals Interactions of rat α-foetoprotein with bilirubin

1979 ◽  
Vol 179 (3) ◽  
pp. 705-707 ◽  
Author(s):  
V Versée ◽  
A O Barel
Keyword(s):  
Absorption Spectrum ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Oxidation Rate ◽  
Bovine Serum ◽  
Bile Pigment ◽  
Binding Parameters ◽  
Enzymic Oxidation ◽  
Bilirubin Binding

The binding of bilirubin to rat-alpha-foetoprotein has been measured by changes in the absorption spectrum and by the appearance of two intense circular-dichroism bands. Furthermore binding of this bile pigment has been demonstrated by a decrease of its enzymic oxidation rate and by competition experiments with bovine serum albumin-agarose. The binding parameters have been determined as follows: n = 1.0 mol bound/mol of protein and Ka = 2.9 × 10(6) M-1. Competition of oestradiol for the bilirubin-binding site has not been established.

scholarly journals In vitro Model for Studying Interactions between Ketorolac and Omeprazole with Bovine Serum Albumin by UV-Spectroscopic Method

2015 ◽  
Vol 17 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Kanij Nahar Deepa ◽  
Md Khalid Hossain ◽  
Md Shah Amran ◽  
Shaila Kabir
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Association Constant ◽  
Spectroscopic Method ◽  
Free Fraction ◽  
In Vivo Model ◽  
Specific Probe

The binding of Ketorolac and Omeprazole to bovine serum albumin (BSA) was studied by equilibrium dialysis method followed by UV spectroscopy. Warfarin and Diazepam were used as site-I and site-II specific probe, respectively. The binding of Ketorolac and Omeprazole was characterized by two sets of association constant: high affinity association constant (K1) with low capacity binding site (n1) and low affinity association constant (K1) with high capacity binding site (n1). In this study, n1 and n1 values were found to be 0.25 ± 0.006 and 1.8 ± 0.025 for Ketorolac and 0.22 ± 0.030 and 1.3±0.035 for Omeprazole at pH 7.4 and 37°C, respectively. At the same condition, the values of K1 and K1 for Ketorolac were found to be 0.624 ± 0.033 ?M-1 and 0.133 ± 0.023 ?M-1 and that of Omeprazole were 0.51 ± 0.001 ?M-1 and 0.28 ± 0.005 ?M-1, respectively. Site specific probe displacement studies implied that both Ketorolac and Omeprazole bind predominantly to site-II, the Diazepam site. In the present study, both Ketorolac and Omeprazole increased the free fraction of each other when they simultaneously bound to BSA. They compete for a common binding site on the albumin molecule, thereby free fraction of both the drugs was increased as compared to the level obtained when the drugs were given individually. We, thus, conclude that during concurrent administration of Ketorolac and Omeprazole adequate precautions should be taken. However, further studies are needed on in-vivo model to substantiate the findings from in-vitro experiments. DOI: http://dx.doi.org/10.3329/bpj.v17i1.22323 Bangladesh Pharmaceutical Journal 17(1): 92-98, 2014

scholarly journals Location of naphthol yellow-S binding site on bovine serum albumin.

1981 ◽  
Vol 4 (11) ◽  
pp. 851-859
Author(s):  
MOTOHARU IWATSURU ◽  
HIDEO NISHIGORI ◽  
KAZUO MARUYAMA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum
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