ArticleJournal of fluorescence2017
Effect of a Synthesized Amyl-Glycine1, 10-Phenanthroline Platinum Nitrate on Structure and Stability of Human Blood Carrier Protein, Albumin: Spectroscopic and Modeling Approaches.
Article in Journal of fluorescence, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Injectable light-assisted thermo-responsive methylcellulose-sodium humate hydrogel proposed for photothermal ablation and localized delivery of cisplatin.Frontiers in bioengineering and biotechnology · 2022Article
- Poly (N-vinylpyrrolidone) modification mitigates plasma protein corona formation on phosphomolybdate-based nanoparticles.Journal of nanobiotechnology · 2021Article
- Investigation of Decitabine Effects on HDAC3 and HDAC7 mRNA Expression in NALM-6 and HL-60 Cancer Cell Lines.Reports of biochemistry & molecular biology · 2021Article
- The Protein-Binding Behavior of Platinum Anticancer Drugs in Blood Revealed by Mass Spectrometry.Pharmaceuticals (Basel, Switzerland) · 2021Review
- A Facile Method to Synthesize 3D Pomegranate-like Polydopamine Microspheres.Frontiers in bioengineering and biotechnology · 2021Article
- NF-κB and NLRP3 gene expression changes during warm hepatic ischemia-reperfusion in rats with and without silibinin.Gastroenterology and hepatology from bed to bench · 2021Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study, biological evaluation of a new synthesized anti-cancer compound, amyl-glycine1, 10-phenanthroline Platinum nitrate (Pt(II) complex), was investigated at different temperatures by spectroscopic methods (far-UV circular dichroism (CD) and fluorescence) and modeling methods (docking and FRET). Human serum albumin (HSA), one of the vital proteins in drug delivery system in the body, was used as a target protein. The Pt(II) complex is able to quench the intrinsic fluorescence of HSA considerably. Binding and thermodynamic parameters of the interaction between the protein and the ligand were analyzed by fluorescence quenching method. The far-UV CD spectra revealed that the secondary structure of HSA did not show any noticeable change upon interaction with Pt(II) complex at both 25 and 37°C. The calculation of fluorescence resonance energy transfer (FRET) confirmed that quenching mechanism is static, and the observed distance between the donor and acceptor is 1.18 nm. Molecular docking results are in agreement with experimental data suggesting that there is one site on HSA at which Pt(II) complex binds spontaneously. Moreover, docking results together with FRET evaluation illustrated that Pt(II) complex is located near Trp214 at a distance of 1.96 nm. Our experimental and theoretical results indicated that the driving forces for Pt(II) complex interaction with HSA are hydrogen bonding and van der Waals interactions. The combination of molecular docking and spectroscopy methods suggested that use of this new Pt(II) complex as an anti-cancer agent, is an effective innovative approach in cancer chemotherapy providing a better understanding of effects of new designed drugs.
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