Effect of temperature on the methotrexate – BSA interaction: Spectroscopic study

Sułkowska, Anna; Maciążek, Małgorzata; Równicka, J.; Bojko, Barbara; Pentak, Danuta; Sułkowski, Wieslaw W.

doi:10.1016/j.molstruc.2006.10.058

Cited by 62 publications

(35 citation statements)

References 24 publications

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“…Moreover, the deshielding eect of the aromatic protons of KP may be caused by the hydrogen bonds formed by NH 2 , OH and SH groups in the structure of the albumin. This is in agreement with the studies described in previous study [11,32]. Furthermore, above the molar ratio KP:HSA 29:1 the position of H16 and H8 resonance signals still shifted towards a higher and lower eld, respectively.…”

Section: 2supporting

confidence: 93%

Comparative Analysis of KP-HSA Complex by Spectroscopic Methods

et al. 2013

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The main objective of the presented study was to characterize the high (HAS) and low anity (LAS) binding sites of ketoprofen (KP) in human serum albumin (HSA) structure with the use of spectrouorescence and proton nuclear magnetic resonance spectroscopy. In vitro uorescence analysis was used to estimate the eect of KP on the HSA uorescence. The association constants Ka [M −1 ] of KP-HSA complex in the HAS were determined with the use of Scatchard, Klotz, and Hill analysis. The quenching KQ [M −1 ] constants were determined on the basis of the SternVolmer equation. Binding of ketoprofen to plasma protein was also studied with the use of 8-anilinonapthalene-1-sulfonic acid (ANS) and 5-dimethylaminonaphthalene-1-sulfonic acid (DNSA) as the uorescence probes in IIIA and IIA subdomains of HSA, respectively. To estimate the cooperativeness in proteins Hill's coecient nH was used. The analysis of proton nuclear magnetic resonance spectra of KP in the presence of HSA allows us to observe the interactions between aromatic rings of the drug and the rings of amino acids located in the hydrophobic subdomains of the protein on the basis of the changes of chemical shifts ∆σ [ppm]

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Section: 2supporting

confidence: 93%

Comparative Analysis of KP-HSA Complex by Spectroscopic Methods

et al. 2013

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“…However, higher temperatures may affect the stability of BSA -drug systems [46]. In our case, increasing temperatures clearly led to lower complex stabilities.…”

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Spectroscopic Analysis of the Binding Interaction Between Tinidazole and Bovine Serum Albumin (BSA)

Shi

Cao

Ren

et al. 2007

Chemistry & Biodiversity

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The interaction between bovine serum albumin (BSA) and tinidazole (Tindamax; 1) in aqueous solution was investigated in detail by means of UV/VIS and fluorescence spectroscopy, as well as through resonance light-scattering (RLS) spectroscopy. The apparent binding constant and number of binding sites were determined at three different temperatures, as well as the average binding distances between 1 and the nearest amino acid residue(s) of BSA, as analyzed by means of Förster's theory of non-radiation energy transfer. Compound 1 was found to quench the inner fluorescence of BSA by forming a tight 1:1 aggregate, based on both static quenching and non-radiation energy transfer. The entropy change upon complexation was positive, and the enthalpy change was negative, indicating that the observed spontaneous binding is mainly driven by electrostatic interactions.

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“…Moreover, the lack of dependence on temperature at higher ZCVI 4 -2/BSA molar ratio leads us to hypothesize that there are additional stabilization factors between the ZCVI 4 -2 and BSA, such as van der Waals forces. 25,26) When comparing the stability of the nanocomplex at two given pH values, we found that the complex showed less temperature dependence at pH 6.8 than that at pH 3.0, thus the nanocomplex was more stable at pH 6.8. This could be explained by the conformational change from pH 6.8 to 3.0, which would be further discussed in the following text.…”

Section: Resultsmentioning

confidence: 97%

Interaction Characteristics with Bovine Serum Albumin and Retarded Nitric Oxide Release of ZCVI4-2, a New Nitric Oxide-Releasing Derivative of Oleanolic Acid

Zhang

Gao

et al. 2011

CHEMICAL & PHARMACEUTICAL BULLETIN

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Human hepatocellular carcinoma (HCC) is one of the leading causes for mortality in the world and there is no effective chemotherapy at present. Therefore, development of new therapeutically effective and low toxic reagents, particularly injectable drugs, will be of great significance. ZCVI 4 -2 ( Fig. 1) is a newly developed furoxan-based nitric oxide-releasing derivative of oleanolic acid, and has been successfully synthesized as galactosyl derivative 3 of the compound 1 (furoxan-based nitric oxide-releasing derivative of oleanolic acid) by Huang et al. 1) As reported previously, it exhibited strong cytotoxicity against HCC in vitro and significantly inhibited the growth of HCC tumors in vivo, indicating that ZCVI 4 -2 may be a promising candidate for the treatment of human HCC. 1) However, ZCVI 4 -2 has a very low aqueous solubility (Ͻ10 mg/ml at pH 3.0-9.0). The poor solubility of ZCVI 4 -2 has been a major hindrance in the development of its parenteral dosage forms. In our previous research, the combination of macrogol 15 hydroxystearate (Solutol HS-15), propylene glycol and ethanol was used to improve its solubility successfully to be up to 5 mg/ml. In vivo activity evaluation indicated that ZCVI 4 -2 treatment with 25 mg/kg of ZCVI 4 -2 enhanced the inhibitory effect on the growth of HCC tumors SMMC-7721 transplanted in nude mice ( pϽ0.01 vs. treatment with 12.5 mg/kg), and its inhibitory effect was similar to that of 5-FU treatment. The tumor weights in the mice treated with ZCVI 4 -2 at 12.5 or 25 mg/kg was significantly lower than that from the vehicletreated controls (pϽ0.01). However, ZCVI 4 -2 injection displayed obvious toxicity to mice in toxicological studies with a LD 50 value of 94.1 mg/kg. 1) By comparing the mice survival of ZCVI 4 -2 suspension with ZCVI 4 -2 injection, it was inferred that the toxicity of ZCVI 4 -2 may be attributed firstly to the fast release of nitric oxide (NO) in blood and secondly to the surfactant and organic solvents in the formulation.The serum albumin was used frequently for the preparation of nanoparticles because of its excellent water-solubility and biocompatibility. Human serum albumin (HSA) had been successfully bound with paclitaxel and formulated into Abraxane ® , the paclitaxel protein-bound particles for injectable suspension. The absence of organic solvents and surfactants significantly improved the clinical safety.2-5) The key step to prepare the protein (bovine serum albumin (BSA) or HSA)-bound nanocomplex is to determine the rational condition for the binding between drug and protein through interaction study. To date, however, the interaction characteristics, the binding condition for paclitaxel and HSA, the screening process of formulation and technology of Abraxane ® were not reported. To delay the release of the NO, and to lower the toxicity after injection, the serum albumin (BSA) was utilized for the preparation of the surfactant-free serum albumin nanocomplexes of ZCVI 4 -2 in this study. The main objective of the present study is to study the in...

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Effect of temperature on the methotrexate – BSA interaction: Spectroscopic study

Cited by 62 publications

References 24 publications

Comparative Analysis of KP-HSA Complex by Spectroscopic Methods

Comparative Analysis of KP-HSA Complex by Spectroscopic Methods

Spectroscopic Analysis of the Binding Interaction Between Tinidazole and Bovine Serum Albumin (BSA)

Interaction Characteristics with Bovine Serum Albumin and Retarded Nitric Oxide Release of ZCVI4-2, a New Nitric Oxide-Releasing Derivative of Oleanolic Acid

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