Effect of Cu2+ and Fe3+ for drug delivery: Decreased binding affinity of ilaprazole to bovine serum albumin

Zhang, Yuping; Shi, Shuyun; Huang, Kelong; Chen, Xiaoqin; Peng, Mijun

doi:10.1016/j.jlumin.2011.05.008

Cited by 22 publications

(20 citation statements)

References 27 publications

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“…In the experiments, flavonoid was first added into the BSA solution for some time, and then pantoprazole was added, therefore, flavonoid first combined with BSA to form flavonoid-BSA complex, and then pantoprazole reacted with flavonoid-BSA complex. Overall, the decreased binding constants of pantoprazole in the presence of flavonoids were consistent with two distinct interpretations (Mote et al, 2010;Zhang, Shi, Huang, Chen, & Peng, 2011): (1) a competitive binding in the flavonoid high-affinity site; (2) a noncompetitive binding in a different albumin site. It was a puzzle about whether the presence of flavonoids affected the binding mode of pantoprazole with BSA.…”

Section: Effect Of Quercetin Luteolin Taxifolin and (+)-Catechin Onsupporting

confidence: 72%

The influence of flavonoids on the binding of pantoprazole to bovine serum albumin by spectroscopic methods: With the viewpoint of food/drug interference

et al. 2012

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Section: Effect Of Quercetin Luteolin Taxifolin and (+)-Catechin Onsupporting

confidence: 72%

The influence of flavonoids on the binding of pantoprazole to bovine serum albumin by spectroscopic methods: With the viewpoint of food/drug interference

et al. 2012

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“…The competitive binding effect will decrease the binding affinity of drugs to protein. The second is conformational changes in proteins induced by metal ions, which will induce easier or more difficult binding of drugs to proteins . The last reason is probably the formation of a metal ion–drug complex, which will increase or decrease the binding affinity of drugs to plasma proteins .…”

Section: Resultsmentioning

confidence: 99%

Enhancement of the binding affinity of methylene blue to site I in human serum albumin by cupric and ferric ions

Wang

et al. 2015

Luminescence

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In this work, the binding characteristics of methylene blue (MB) to human serum albumin (HSA) and the influence of Cu(2+) and Fe(3+) on the binding affinity of MB to HSA were investigated using fluorescence, absorption, circular dichroism (CD) spectroscopy and molecular modelling. The results of competitive binding experiments using the site probes ketoprofen and ibuprofen as specific markers suggested that MB was located in site I within sub-domain IIA of HSA. The molecular modelling results agreed with the results of competitive site marker experiments and the results of CD spectra indicated that the interaction between MB and HSA caused the conformational changes in HSA. The binding affinity of MB to HSA was enhanced but to a different extent in the presence of Cu(2+) and Fe(3+), respectively, which indicated that the influence of different metal ions varied. Enhancement of the binding affinity of MB to HSA in the presence of Cu(2+) is due to the formation of Cu(2+)-HSA complex leading to the conformational changes in HSA, whereas in the presence of Fe(3+), enhancement of the binding affinity is due to the greater stability of the Fe(3+)-HSA-MB complex compared with the MB-HSA complex.

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“…Therefore, Föster's energy transfer theory is often used to calculate the distance between amino acid residues on proteins and drugs in the binding sites, which will happen under these conditions [33]: (i) the donor can produce fluorescence light, (ii) the donor's fluorescence emission spectrum overlaps the UV-vis absorbance spectrum of the acceptor, and (iii) the distance between donor and acceptor is small (1-10 nm). The efficiency of energy transfer, E, is calculated according to Föster's energy transfer theory [34].…”

Section: Energy Transfer Between Scopoletin and Bsa/hsamentioning

confidence: 99%

Studies on the interaction between scopoletin and two serum albumins by spectroscopic methods

Cheng

2012

Journal of Luminescence

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Effect of Cu2+ and Fe3+ for drug delivery: Decreased binding affinity of ilaprazole to bovine serum albumin

Cited by 22 publications

References 27 publications

The influence of flavonoids on the binding of pantoprazole to bovine serum albumin by spectroscopic methods: With the viewpoint of food/drug interference

The influence of flavonoids on the binding of pantoprazole to bovine serum albumin by spectroscopic methods: With the viewpoint of food/drug interference

Enhancement of the binding affinity of methylene blue to site I in human serum albumin by cupric and ferric ions

Studies on the interaction between scopoletin and two serum albumins by spectroscopic methods

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