Effects of γ‐Irradiation on the Molecular Structures and Functions of Human Serum Albumin

Hu, Xinxin; Song, Wei; Li, Wei; Guo, Chengxiang; Zhang, Yu; Liu, Rutao

doi:10.1002/jbt.21818

Cited by 7 publications

(1 citation statement)

References 43 publications

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“…Activity of HSA. HSA has esterase activity, can hydrolyze pNPA to produce p-nitrophenol, and has the maximum absorption at 400 nm [56]. Te esterase activity of HSA decreases with the increase of pyrazine concentration (Figure 14(a)).…”

Section: Te Efect Of Diferent Pyrazines On the Physiologicalmentioning

confidence: 99%

Interaction and Binding Kinetics of Different Substituted Pyrazines with HSA: Based on Multispectral, Physiological Activity, and Molecular Dynamics Simulations

Tong,

Wang,

et al. 2024

Journal of Food Biochemistry

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Pyrazine is a kind of compound containing pyrazine ring structure, which has attracted the attention of researchers because of its special aroma and healthcare function. It is currently used in spices, pharmaceuticals, food additives, and other industries. Human serum albumin (HSA) is a transport and storage protein in the human circulatory system. Previous research reported that pyrazine can interact with albumin, but the interaction between pyrazine and HSA has not been reported. Consequently, this study is based on the multispectral method and molecular dynamics (MD) simulation, exploring the interaction between different pyrazines and HSA. The results show that the four pyrazines mainly quench the endogenous fluorescence of HSA through the static quenching mechanism. Molecular docking indicates that hydrophobic forces play a major role in the binding of pyrazines with HSA. At the same time, synchronous fluorescence spectroscopy, circular dichroism (CD), three-dimensional fluorescence spectroscopy, and resonance light scattering (RLS) showed that each pyrazine compound can change the conformation of HSA. MD simulation results show that the combination of four pyrazines and HSA can enhance the stability of HSA. Among them, 2,3,5,6-tetramethylpyrazine (TTMP) and 2,3,5-trimethylpyrazine (TMTP) binding is the most stable and the most unstable combination with HSA, respectively. In addition, the four pyrazines could affect the physiological activity of HSA. This study is of great significance to explore the mechanism of action of pyrazine compounds in vivo and can provide useful information for the application of pyrazine compounds in food.

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Section: Te Efect Of Diferent Pyrazines On the Physiologicalmentioning

confidence: 99%

Interaction and Binding Kinetics of Different Substituted Pyrazines with HSA: Based on Multispectral, Physiological Activity, and Molecular Dynamics Simulations

Tong,

Wang,

et al. 2024

Journal of Food Biochemistry

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Cytosine arabinoside prodrug designed to bind plasma serum albumin for drug delivery

Wei

Zhang

Yang

et al. 2018

Drug Deliv. and Transl. Res.

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Rational design of anticancer prodrugs for efficient albumin binding can show distinct advantages in drug delivery in terms of high drug availability, long systemic circulation, potential targeting effect, and enhanced chemotherapy effect. In the present study, we reported a cytosine arabinoside (Ara-C) prodrug which could well formulate in solution and instantly transform into long-circulating nanocomplexes by hitchhiking blood-circulating albumin after i.v. administration. Specifically, Ara-C was conjugated with an albumin-binding maleimide derivative, the resulting Ara-C maleimide caproic acid conjugate (AM) was well formulated in aqueous solution, conferring high albumin-binding ability in vitro albumin-binding studies. Moreover, in vivo fluorescence images of sulfo-cyanine5 maleimide indirectly demonstrated that AM showed better accumulation in tumors, exhibiting superior tumor targeting ability and antitumor activity compared to Ara-C. Such a uniquely developed strategy, integrating high albumin-binding capability, has great potential to be applied in clinical cancer therapy.

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Protective effects of curcumin against gamma ray induced conformational change of human serum albumin

Kar

Basak

Ghosh

et al. 2017

International Journal of Biological Macromolecules

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Effects of γ‐Irradiation on the Molecular Structures and Functions of Human Serum Albumin

Cited by 7 publications

References 43 publications

Interaction and Binding Kinetics of Different Substituted Pyrazines with HSA: Based on Multispectral, Physiological Activity, and Molecular Dynamics Simulations

Interaction and Binding Kinetics of Different Substituted Pyrazines with HSA: Based on Multispectral, Physiological Activity, and Molecular Dynamics Simulations

Cytosine arabinoside prodrug designed to bind plasma serum albumin for drug delivery

Protective effects of curcumin against gamma ray induced conformational change of human serum albumin

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