Study of the interaction of artemisinin with bovine serum albumin

Bian, He‐Dong; Li, Mei; Yu, Qing; Chen, Zhen-Feng; Tian, Jianniao; Liang, Hong

doi:10.1016/j.ijbiomac.2006.04.008

Cited by 68 publications

(54 citation statements)

References 38 publications

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“…Joseph et al, investigated the effect of the glycation of albumin on its binding to warfarin, which is often used as a probe compound for Sudlow site I, and reported no significant changes in the binding affinity of warfarin to glycated albumin, whereas a 4.7-5.8 fold increase in the binding affinity to glycated albumin was observed in L-tryptophan, a probe for Sudlow site II [13]. Bian et al, examined the interaction between artemisinin and albumin and demonstrated that artemisinin could bind to site I [22]. Taking these findings and the structural similarities between of AS and DHA to artemisinin into consideration, AS and DHA can also bind to site I of albumin; therefore, their bindings to albumin may not be affected by its glycation.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of efficacy and safety of artesunate and its active metabolite, dihydroartemisinin, in streptozotocin-induced diabetes rats by blood pharmacokinetic analysis

Fukushima¹,

Uchimura²,

Okada³

et al. 2014

Interact Med Chem

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Background: Artesunate (AS), an anti-malarial drug, is hydrolyzed by serum esterase for its conversion to the active metabolite, dihydroartemisinin (DHA). Evidence for the clinical effectiveness of AS is growing; however, little information is available on special populations such as patients with diabetes mellitus (DM). In addition, although erythrocytes are considered as a target site, the blood pharmacokinetics of AS and DHA remain unclear. Therefore, the blood pharmacokinetics of AS and DHA were investigated in DM rats in the present study. Methods: DM rats were prepared by intraperitoneal injection of streptozotocin. An in vitro protein binding study of AS and DHA was performed by the ultrafiltration method. Plasma and blood samples were collected after the intravenous administration of AS, to analyze pharmacokinetics of AS and DHA. Blood to plasma ratios (BP ratio), as an index of erythrocyte distribution, were then calculated by dividing blood concentrations by plasma concentrations. Results: The protein bindings of AS and DHA were 83.7% and 92.6% in control rats and 86.2% and 92.2% in DM rats, respectively. All concentration profiles in this study were best fit by a two compartment model; the plasma and blood pharmacokinetic parameters of AS and DHA in DM rats were not significantly different from those in control rats. The BP ratio of AS was at an extremely low level (approximately 0.5) just after its administration, whereas that of DHA was maintained above 1.0 throughout the study; however, no significant changes were observed between control and DM rats. Conclusion:The glycation of albumin with DM did not affect the protein bindings of AS or DHA. No significant changes were observed in the conversion of AS to DHA by serum esterase or disposition of DHA in DM rats. The blood concentrations of DHA declined in parallel with plasma concentrations and the distribution of DHA to erythrocytes was good. In conclusion, the efficacy and safety of both AS and DHA were tolerated in DM rats with DHA having more favorable characteristics than AS.

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Section: Discussionmentioning

confidence: 99%

Evaluation of efficacy and safety of artesunate and its active metabolite, dihydroartemisinin, in streptozotocin-induced diabetes rats by blood pharmacokinetic analysis

Fukushima¹,

Uchimura²,

Okada³

et al. 2014

Interact Med Chem

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“…As listed in Table 3, the apparent binding constants between Ru-TSC anticancer drug and HSA decreased when common metal ions were present, which might be due to the inhibition of the binding interaction between Ru-TSC anticancer drug and HSA after the addition of common metal ions. These results suggested the shortening of the storage time of Ru-TSC anticancer drug in blood plasma and the requirement of more doses of Ru-TSC anticancer drug to achieve the desired therapeutic effect [37,38].…”

Section: Effects Of Common Metal Ions On the Apparent Binding Constantmentioning

confidence: 95%

“…Some metal ions existed in plasma could affect the reactions of drugs and serum albumins [37], so the influence of common metal ions (such as Ag + , K + , Na + , Cu 2+ , Ca 2+ , Mg 2+ , Ni 2+ , Co 2+ , and Fe 3+ ) on the apparent binding constants of HSA-Ru-TSC anticancer drug system was investigated at 298 K. The concentrations of adopted metal ions were the same with the concentration of HSA. As listed in Table 3, the apparent binding constants between Ru-TSC anticancer drug and HSA decreased when common metal ions were present, which might be due to the inhibition of the binding interaction between Ru-TSC anticancer drug and HSA after the addition of common metal ions.…”

Section: Effects Of Common Metal Ions On the Apparent Binding Constantmentioning

confidence: 99%

Thermodynamic Investigation of Interaction Between [(η 6-p-Cymene) RuII(Acetone-N 4-Phenylthiosemicarbazone)Cl]Cl Anticancer Drug and Human Serum Albumin: Spectroscopic and Electrochemical Studies

Huang

Zhu

Qian

et al. 2014

Biol Trace Elem Res

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In this contribution, the interaction between [(η (6)-p-cymene)Ru(II)(acetone-N (4)-phenylthiosemicarbazone)Cl]Cl (Ru-TSC) anticancer drug and human serum albumin (HSA) was investigated by spectroscopic and electrochemical techniques. The fluorescence spectra results indicated that Ru-TSC anticancer drug could quench the intrinsic fluorescence of HSA through dynamic quenching mode. The calculated corresponding activation energy of the interaction between Ru-TSC anticancer drug and HSA was 35.62 kJ mol(-1). The distance between HSA and Ru-TSC anticancer drug was obtained according to fluorescence resonance energy transfer. The results of synchronous fluorescence spectra, three-dimensional fluorescence spectra, Fourier transform infrared spectroscopy (FTIR) spectra, and circular dichroism (CD) spectra indicated that the microenvironment and the conformation of HSA were all changed in the presence of Ru-TSC anticancer drug. The results of cyclic voltammetry further validated the interaction between Ru-TSC and HSA. These results indicated that the biological activity of HSA was affected by Ru-TSC anticancer drug dramatically.

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“…The ligands can simultaneously bind to BSA by competitive binding and non-competitive binding mechanism. To recognize the binding region of triptolide upon BSA, the site probes ibuprofen and phenylbutazone, which are specifically bound to the known region or site on BSA (Sreerama and Woody, 1993;Bian, et al, 2006), are chosen for the site marker competition experiments. The data were analyzed employing the Equation 3.…”

Section: Binding Mode and Binding Site Between Triptolide And Bsa Sitmentioning

confidence: 99%

Studies on the Interaction Between Triptolide and Bovine Serum Albumin (Bsa) by Spectroscopic and Molecular Modeling Methods

Wang¹,

Shi²,

Pang³

et al. 2016

Afr J Tradit Complement Altern Med

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Background: Triptolide is a major active constituent isolated from Tripterygiumwilfordii Hook F, a Chinese herbal medicine. This study investigated the intermolecular interaction between triptolide and bovine serum albumin (BSA). Materials and Methods:The fluorescence, circular dichroism (CD) and molecular docking methods were used to investigate the intermolecular interaction between triptolide and BSA. The binding constant, the number of binding sites, binding subdomain and the thermodynamic parameters were measured. Results: The results of this experiment revealed that the intrinsic fluorescence of BSA was effectively quenched by triptolide via static quenching. The experimental results of synchronous fluorescence and CD spectra showed that the conformation of BSA was changed in the presence of triptolide. Conclusion: It indicated that triptolide could spontaneously bind on site II (subdomain IIIA) of BSA mainly via hydrogen bonding interactions and Van der Waals force.

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Study of the interaction of artemisinin with bovine serum albumin

Cited by 68 publications

References 38 publications

Evaluation of efficacy and safety of artesunate and its active metabolite, dihydroartemisinin, in streptozotocin-induced diabetes rats by blood pharmacokinetic analysis

Evaluation of efficacy and safety of artesunate and its active metabolite, dihydroartemisinin, in streptozotocin-induced diabetes rats by blood pharmacokinetic analysis

Thermodynamic Investigation of Interaction Between [(η 6-p-Cymene) RuII(Acetone-N 4-Phenylthiosemicarbazone)Cl]Cl Anticancer Drug and Human Serum Albumin: Spectroscopic and Electrochemical Studies

Studies on the Interaction Between Triptolide and Bovine Serum Albumin (Bsa) by Spectroscopic and Molecular Modeling Methods

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