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December 23, 2014RSC Advances

Biophysical investigation of thymoquinone binding to ‘N’ and ‘B’ isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity

Mohd Ishtikhar Gulam Rabbani Shawez Khan Rizwan Hasan Khan

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Abstract

Thymoquinone more strongly interacts with the ‘N’ isoform in comparison to the ‘B’ isoform of HSA and also increases its thermal stability but the antioxidant activity is significantly higher at the ‘B’ isoform of HSA.

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Cite This Study

Ishtikhar et al. (2014) studied this question.

synapsesocial.com/papers/6aae31ccaf16b36679cd5c2d https://doi.org/10.1039/c4ra09892g

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Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Thymoquinone in the clinical treatment of cancer: Fact or fiction?Human Clinical Trial · 2013 · 88 citations
2Antitubercular and Antibacterial Activity of Quinonoid Natural Products Against Multi‐Drug Resistant Clinical IsolatesOriginal Research · 2013 · 101 citations
3Reversible Denaturation of Human Serum Albumin by pH, Temperature, and Guanidine Hydrochloride Followed by Optical RotationOriginal Research · 1973 · 188 citations
4Aqueous Solubility and Degradation Kinetics of the Phytochemical Anticancer Thymoquinone; Probing the Effects of Solvents, pH and LightOriginal Research · 2014 · 168 citations
5Anticancer Effects of Thymoquinone, Caffeic Acid Phenethyl Ester and Resveratrol on A549 Non-small Cell Lung Cancer Cells Exposed to Benzo(a)pyreneOriginal Research · 2013 · 91 citations

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