ArticleDrug design, development and therapy2018
Spectroscopic and molecular modeling studies of binding interaction between bovine serum albumin and roflumilast.
Article in Drug design, development and therapy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed, 54 citations in OpenAlex.
- Proteins for Polyphenol Encapsulation, Functional Food Production, and Breast Cancer Incidence Reduction: Impact of pH Conditions, BSA Particle Size, and Curcumin Concentration.The protein journal · 2026Review
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- Interaction of Ibuprofen with Partially Unfolded Bovine Serum Albumin in the Presence of Ionic Micelles and Oligosaccharides at Different λACS omega · 2023Article
- Magnolol and Luteolin Inhibition of α-Glucosidase Activity: Kinetics and Type of Interaction Detected by In Vitro and In Silico Studies.Pharmaceuticals (Basel, Switzerland) · 2022Article
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- Mechanistic interaction study of 5,6-Dichloro-2-[2-(pyridin-2-yl)ethyl]isoindoline-1,3-dione with bovine serum albumin by spectroscopic and molecular docking approaches.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2019Article
- Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe binding interaction between bovine serum albumin (BSA) and roflumilast (ROF) was explored in this study. The binding of drugs to albumin plays a vital role in their pharmacokinetics and pharmacodynamics in vivo. The mechanisms involved in the interaction between BSA and ROF was studied using multi-spectroscopic experimental and computational approaches. MATERIALS AND
methodsSpectrofluorometric experiments were used to determine the method of quenching involved and the conformational changes in the BSA. UV-visible spectroscopy synchronous and three-dimensional fluorescence spectroscopy were used to further explore the binding interaction mechanism.
resultsThe results suggested that the intrinsic fluorescence of BSA was quenched due to the formation of a static complex between ROF and BSA. Conformational changes in BSA were determined based on its interaction with ROF. The thermodynamic results suggested that the interaction between ROF and BSA was spontaneous and a hydrophobic interaction occurred between them. Site I of BSA was suggested as the site of interaction between ROF and BSA based on the site marker experiments.
conclusionThe molecular simulation results and the experimental outcomes were complimentary to each other and helped to identify the binding site and nature of bonds involved in the interaction between ROF and BSA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.