ArticleFrontiers in chemistry2018
Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach.
Article in Frontiers in chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 121 citations in OpenAlex.
- Tryptophan-Mediated Sodium Dodecyl Sulfate Binding to Proteins.The protein journal · 2026Article
- Synthesis of tetrazole based donor-acceptor type fluorescent molecules and their interaction with transport protein bovine serum albumin.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026Article
- Probing the Interaction Between Thioacetamide Fungicide and Bovine Serum Albumin Through Fluorescence, Electrochemical, and Docking Analyses.Luminescence : the journal of biological and chemical luminescence · 2026Article
- Ultrabright NIR-II Nanoprobes forACS nanoscience Au · 2025Article
- Molecular interaction study of L-Ornithine with bovine serum albumin using spectroscopic and molecular docking methods.Scientific reports · 2025Article
- A method for estimation of plasma protein binding using diffusion ordered NMR spectroscopy (DOSY).RSC medicinal chemistry · 2024Article
- Interaction mechanism of oseltamivir phosphate with bovine serum albumin: multispectroscopic and molecular docking study.BMC chemistry · 2024Article
- Article
- Profiling the Interaction between Human Serum Albumin and Clinically Relevant HIV Reverse Transcriptase Inhibitors.Viruses · 2024Article
- Removal of bromophenol blue from polluted water using a novel azo-functionalized magnetic nano-adsorbent.RSC advances · 2024Article
- Neratinib for HER2-positive breast cancer with an overlooked option.Molecular medicine (Cambridge, Mass.) · 2023Review
- Dual targeting multiwalled carbon nanotubes for improved neratinib delivery in breast cancer.RSC advances · 2023Article
- Interactions ofMembranes · 2023Article
- Article
- Interaction of Ibuprofen with Partially Unfolded Bovine Serum Albumin in the Presence of Ionic Micelles and Oligosaccharides at Different λACS omega · 2023Article
- A study of structure-activity relationship and anion-controlled quinolinyl Ag(I) complexes as antimicrobial and antioxidant agents as well as their interaction with macromolecules.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
- Neratinib causes non-recoverable gut injury and reduces intestinal cytochrome P450 3A enzyme in mice.Toxicology research · 2022Article
- Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA.Molecules (Basel, Switzerland) · 2021Article
- A New Electrochemical Platform for Dasatinib Anticancer Drug Sensing Using FeMicromachines · 2021Article
- Recent Advances of Taxol-Loaded Biocompatible Nanocarriers Embedded in Natural Polymer-Based Hydrogels.Gels (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA). Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR) and molecular docking experiments were performed to study this interaction. The fluorescence of BSA is attributed to the presence of tryptophan (Trp) residues. The fluorescence of BSA in presence of neratinib was studied using the excitation wavelength of 280 nm and the emission was measured at 300-500 nm at three different temperatures. Neratinib quenched the BSA intrinsic fluorescence by static mechanism. A complex formation occurred due to the interaction leading to BSA absorption shift. The fluorescence, UV- absorption, three dimensional fluorescence and FT-IR data showed conformational changes occurred in BSA after interaction with neratinib. The binding constant values decreased as the temperature increased suggesting an instable complex formation at high temperature. Site I (sub-domain IIA) was observed as the principal binding site for neratinib. Hydrogen bonding and Van der Waals forces were suggested to be involved in the BSA-neratinib interaction due to the negative values of entropy and enthalpy changes.
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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.