ArticleJournal of fluorescence2015
Investigation of the binding between pepsin and nucleoside analogs by spectroscopy and molecular simulation.
Article in Journal of fluorescence, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Investigation of the Interaction between 1,3-Diazaheterocyclic Compounds and the Fat Mass and Obesity-Associated Protein by Fluorescence Spectroscopy and Molecular Modeling.Journal of fluorescence · 2017Article
- Spectroscopy and Molecular Modeling Study on the Interaction Between Mycophenolate Mofetil and Pepsin.Journal of fluorescence · 2016Article
- Influence of the Ring Size on the Binding Ability of FTO Investigated by Fluorescence Spectroscopy.Journal of fluorescence · 2015Article
- Interaction Behavior Between Niclosamide and Pepsin Determined by Spectroscopic and Docking Methods.Journal of fluorescence · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper, the interactions of pepsin with CYD (cytidine) or nucleoside analogs, including FNC (2'-deoxy-2'-β-fluoro-4'-azidocytidine) and CMP (cytidine monophosphate), were investigated by fluorescence, UV-visible absorption and synchronous fluorescence spectroscopy under mimic physiological conditions. The results indicated that FNC (CYD/CMP) caused the fluorescence quenching by the formation of complex. The binding constants and thermo-dynamic parameters at three different temperatures were obtained. The hydrophobic and electrostatic interactions were the predominant intermolecular forces to stabilize the complex. The F atom in FNC might weaken the binding of nucleoside analog to pepsin. Results showed that CYD was the strongest quencher and bound to pepsin with higher affinity.
Indexed as
Identifiers
25721993What OpenQuestion holds
Registered trials
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