ArticlePloS one2011
Interaction of the anticancer plant alkaloid sanguinarine with bovine serum albumin.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 92 citations in OpenAlex.
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- Evaluation of the selectivity of G-quadruplex ligands in living cells with a small molecule fluorescent probe.Analytica chimica acta: X · 2019Article
- Substitution at the C-3 Position of Catechins Has an Influence on the Binding Affinities against Serum Albumin.Molecules (Basel, Switzerland) · 2017Article
- Analysis of the Interaction of Dp44mT with Human Serum Albumin and Calf Thymus DNA Using Molecular Docking and Spectroscopic Techniques.International journal of molecular sciences · 2016Article
- Interaction of Di-2-pyridylketone 2-pyridine Carboxylic Acid Hydrazone and Its Copper Complex with BSA: Effect on Antitumor Activity as Revealed by Spectroscopic Studies.Molecules (Basel, Switzerland) · 2016Article
- Natural isoquinoline alkaloids: binding aspects to functional proteins, serum albumins, hemoglobin, and lysozyme.Biophysical reviews · 2015Review
- Human Serum Albumin Increases the Stability of Green Tea Catechins in Aqueous Physiological Conditions.PloS one · 2015Article
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- Influence of Solvent Polarity and DNA-Binding on Spectral Properties of Quaternary Benzo[c]phenanthridine Alkaloids.PloS one · 2015Article
- Molecular interaction mechanism between 2-mercaptobenzimidazole and copper-zinc superoxide dismutase.PloS one · 2014Article
- Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.PloS one · 2014Article
- Characterization of the interaction between eupatorin and bovine serum albumin by spectroscopic and molecular modeling methods.International journal of molecular sciences · 2013Article
- Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.PloS one · 2013Article
- Spectroscopic investigations on the interactions of potent platinum(II) anticancer agents with bovine serum albumin.Journal of chemical biology · 2012Article
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- DNA abasic site-selective enhancement of sanguinarine fluorescence with a large emission shift.PloS one · 2012Article
- Binding of tetracycline and chlortetracycline to the enzyme trypsin: spectroscopic and molecular modeling investigations.PloS one · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundInteraction of the iminium and alkanolamine forms of sanguinarine with bovine serum albumin (BSA) was characterized by spectroscopic and calorimetric techniques. METHODOLOGY/PRINCIPAL
findingsFormation of strong complexes of BSA with both iminium and alkanolamine forms was revealed from fluorescence quenching of sanguinarine. Binding parameters calculated from Stern-Volmer quenching method revealed that the neutral alkanolamine had higher affinity to BSA compared to the charged iminium form. Specific binding distances of 3.37 and 2.38 nm between Trp 212 (donor) and iminium and alkanolamine forms (acceptor), respectively, were obtained from Forster resonance energy transfer studies. Competitive binding using the site markers warfarin and ibuprofen, having definite binding sites, demonstrated that both forms of sanguinarine bind to site I (subdomain IIA) on BSA. Sanguinarine binding alters protein conformation by reducing the α-helical organization and increasing the coiled structure, indicating a small but definitive partial unfolding of the protein. Thermodynamic parameters evaluated from isothermal titration calorimetry suggested that the binding was enthalpy driven for the iminium form but favoured by negative enthalpy and strong favourable entropy contributions for the alkanolamine form, revealing the involvement of different molecular forces in the complexation. CONCLUSIONS/SIGNIFICANCE: The results suggest that the neutral alkanolamine form binds to the protein more favourably compared to the charged iminium, in stark contrast to the reported DNA binding preference of sanguinarine.
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