A study on the interaction between CdTe quantum dots and chymotrypsin using optical spectroscopy

Peng, Juanjuan; Liu, Shaopu; Yan, Shuguang; Fan, Xuejun; He, Yonghong

doi:10.1016/j.colsurfa.2010.01.027

Cited by 33 publications

(18 citation statements)

References 30 publications

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“…3(B), the binding constants K a at different temperatures were obtained as listed in Table 1 and the order of magnitude was 10 4 . These results showed that the values of K a have a tendency to decrease with the increase in temperature, which indicated that an unstable complex has formed between CdSe NP and BSA and the increasing temperature would lower the stability of the complex [31]. Thus it was deduced that CdSe NP and BSA formed a complex, which led to the decrease of fluorescence intensity of BSA.…”

Section: Fluorescence Bsa Quenching By Cdse Npmentioning

confidence: 78%

Probing the interaction of flower-like CdSe nanostructure particles targeted to bovine serum albumin using spectroscopic techniques

Fan

Liu

et al. 2011

Journal of Luminescence

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Section: Fluorescence Bsa Quenching By Cdse Npmentioning

confidence: 78%

Probing the interaction of flower-like CdSe nanostructure particles targeted to bovine serum albumin using spectroscopic techniques

Fan

Liu

et al. 2011

Journal of Luminescence

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“…Therefore, the RLS intensity of the α‐ChT‐CdCl 2 system was greatly enhanced due to the increase of the surface area of α‐ChT upon CdCl 2 binding and the associate formed by α‐ChT and CdCl 2 . Peng et al obtained similar results and found an increase of the molecular volume when investigating the interaction of CdTe quantum dots with chymotrypsin.…”

Section: Resultsmentioning

confidence: 84%

A study on the interaction between cadmium and α‐chymotrypsin and the underlying mechanisms

Wang

Zheng

Wang

et al. 2018

J Biochem & Molecular Tox

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Because cadmium might interact with proteins and, thus, exert toxicity in organisms, it is vital to understand the molecular mechanism of the interaction between cadmium and biologically relevant proteins as well as the structural and functional changes in these proteins. In this study, the interaction between α-chymotrypsin (α-ChT) and cadmium chloride (CdCl 2 ) was investigated by performing enzyme activity determinations, multispectroscopic measurements, isothermal titration calorimetry, and molecular docking studies. It was demonstrated that CdCl 2 binds to α-ChT mainly via electrostatic forces with (21.0 ± 0.982) binding sites, leading to the increase of α-helix and the decrease of β-sheet. The interaction between CdCl 2 and α-ChT loosened the protein skeleton and increased the molecular volume of α-ChT. CdCl 2 first binds to the interface of α-ChT and then interacts with the key residues His 57 or Asp 102 or both in the active sites, leading to the activity inhibition of α-ChT under the exposure of high CdCl 2 concentrations. K E Y W O R D S cadmium, enzymatic activity, protein structure, α-chymotrypsin (α-ChT) J Biochem Mol Toxicol. 2019;33:e22248. wileyonlinelibrary.com/journal/jbt Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Wang J, Zheng X, Wang W, Guo H, Liu R, Zong W. A study on the interaction between cadmium and α-chymotrypsin and the underlying mechanisms.

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“…In the presence of BPTI, the two lifetime components of HSA were measured as 2.384 and 6.249 ns; for BFDI, the values were 2.408 and 2.545 ns, and for BDTI they were 6.281 and 6.297 ns. Compared with the blank HSA, there was no obvious change in the mean fluorescence lifetime of HSA (from 5.817 ns to 5.811/5.798/5.785 ns), which demonstrated that quenching followed static mechanism .…”

Section: Resultsmentioning

confidence: 88%

Interaction of human serum albumin with novel imidazole derivatives studied by spectroscopy and molecular docking

et al. 2015

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This study was a detailed characterization of the interaction of a series of imidazole derivatives with a model transport protein, human serum albumin (HSA). Fluorescence and time-resolved fluorescence results showed the existence of a static quenching mode for the HSA-imidazole derivative interaction. The binding constant at 296 K was in the order of 10(4) M(-1), showing high affinity between the imidazole derivatives and HSA. A site marker competition study combined with molecular docking revealed that the imidazole derivatives bound to subdomain IIA of HSA (Sudlow's site I). Furthermore, the results of synchronous, 3D, Fourier transform infrared, circular dichroism and UV-vis spectroscopy demonstrated that the secondary structure of HSA was altered in the presence of the imidazole derivatives. The specific binding distance, r, between the donor and acceptor was obtained according to fluorescence resonance energy transfer.

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A study on the interaction between CdTe quantum dots and chymotrypsin using optical spectroscopy

Cited by 33 publications

References 30 publications

Probing the interaction of flower-like CdSe nanostructure particles targeted to bovine serum albumin using spectroscopic techniques

Probing the interaction of flower-like CdSe nanostructure particles targeted to bovine serum albumin using spectroscopic techniques

A study on the interaction between cadmium and α‐chymotrypsin and the underlying mechanisms

Interaction of human serum albumin with novel imidazole derivatives studied by spectroscopy and molecular docking

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