NMR, multi-spectroscopic and molecular modeling approach to investigate the complexes between C.I. Acid Orange 7 and human serum albumin in vitro

Zhou, Xi; Yang, Qiao; Xie, Xiaofeng; Hu, Qin; Qi, Feng‐Ming; Rahman, Zia Ur; Chen, Xingguo

doi:10.1016/j.dyepig.2011.08.012

Cited by 31 publications

(13 citation statements)

References 33 publications

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“…At the molar ratio HSA–paclitaxel (1:5), the spectral shifting changes were observed for HSA amide I band from 1650.0 to 1661.3/cm and amide II band from 1546.3 to 1555.4/cm in the spectrum of HSA–drug complex. The results suggested that the shifts of the amide I and II bands was due to the drug binding to the C = O, C‐N and N‐H groups of protein . These phenomena also indicated that the percentage content of protein α‐helical structure reduced at this molecular ratio.…”

Section: Resultsmentioning

confidence: 92%

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

Yang

Yuan

et al. 2013

Luminescence

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The interaction of paclitaxel with human serum albumin (HSA) was studied using fluorescence, resonance light scattering, ultraviolet-visible, circular dichroism and Fourier transform infrared spectroscopy at pH 7.4. Fluorescence data revealed that the fluorescence quenching of HSA by paclitaxel was a static quenching procedure. Time-resolved fluorescence data also confirmed the quenching mode, which present a constant decay time of about 5 ns. The binding sites were approximately 1 and the binding constant suggested a weak association (324/M at 298 K), which is helpful for the release of the drug to targeted organs. The thermodynamic parameters, ΔG(○), ΔH° and ΔS° were calculated as - 1.06 × 10(4) J/mol, 361 J/mol per K and 9.7 × 10(4) J/mol respectively at 298 K, suggesting that binding was spontaneous and was driven mainly by hydrophobic interactions. The binding distance between HSA and paclitaxel was determined to be 2.23 nm based on the Förster theory. Analysis of circular dichroism, ultraviolet-visible, three-dimensional fluorescence, Fourier transform infrared and resonance light scattering spectra demonstrated that HSA conformation was slightly altered in the presence of paclitaxel and dimension of the individual HSA molecules were larger after interacting with paclitaxel. These results were confirmed by a molecular docking study.

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Section: Resultsmentioning

confidence: 92%

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

Yang

Yuan

et al. 2013

Luminescence

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“…As can be seen from Table , the number of PL molecules bound to HSA was respectively 1.7, 3.2, 6.8, and 8.1 at 293, 298, 303 and 308 K. These results showed that more than one PL molecule could co‐operative bind per protein molecule, which supported that the explanation of positive deviation of the Stern–Volmer plots. Similar situations have been reported in the literature for diacetyl maslinic acid–BSA, AO7–HSA, morin–HSA, [Cr(phen) 2 (dppz)] 3+ –HSA/BSA, and puerarin–HSA complexes . From the viewpoint of drug delivery, an increased temperature may facilitate the binding of PL to the carrier HSA.…”

Section: Resultsmentioning

confidence: 95%

Spectroscopic investigation of the anticancer alkaloid piperlongumine binding to human serum albumin from the viewpoint of drug delivery

Liu

Wang

et al. 2017

Luminescence

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Piperlongumine (PL) is a very promising natural agent with a high potential for cancer treatment. To overcome the poor water solubility of PL, there is a need to develop a novel water-soluble formulation in which PL is non-covalently bound to human serum albumin (HSA). PL binding to HSA was studied by various spectroscopic techniques under simulated physiological conditions. Spectroscopic evidence showed that the interaction of PL with HSA could form a PL-HSA complex. The binding constant (K ) values increased with increasing temperature, and a similar dependence was observed for the number of binding sites (n) values. The number of PL molecules bound to HSA reached 8.1 when the temperature was raised to 308 K. Thermodynamic calculation results suggested that the binding reaction occurred spontaneously but was an entropy-driven process, and hydrophobic forces played a major role in stabilizing the complex. Furthermore, PL binding induced conformational and microenvironmental changes in HSA. Displacement studies indicated that PL and warfarin had separate binding regions in site I. Therefore, it would be possible to develop a novel water-soluble formulation involving PL and HSA. This study may provide some valuable information in terms of improving the poor water solubility of PL.

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“…2A). Meanwhile, the concomitant red-shift (Dl = 7 nm) of the emission peak was observed, indicating the polarity increase and the hydrophobicity decrease of the tryptophan residues along binding to diazotized CLB [48]. Notably, the fluorescence emission at 610 nm for gold NCs was significantly quenched either with the gradual addition of diazotized CLB (Fig.…”

Section: Fluorescence Quenching Of Auncs@bsa Induced By the Diazotizementioning

confidence: 86%

A dual-responsive fluorescence method for the detection of clenbuterol based on BSA-protected gold nanoclusters

Cao

Lian

et al. 2015

Analytica Chimica Acta

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NMR, multi-spectroscopic and molecular modeling approach to investigate the complexes between C.I. Acid Orange 7 and human serum albumin in vitro

Cited by 31 publications

References 33 publications

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

Spectroscopic investigation of the anticancer alkaloid piperlongumine binding to human serum albumin from the viewpoint of drug delivery

A dual-responsive fluorescence method for the detection of clenbuterol based on BSA-protected gold nanoclusters

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