ArticleJournal of pharmaceutical analysis2013
Investigation of the interaction between indigotin and two serum albumins by spectroscopic approaches.
Article in Journal of pharmaceutical analysis, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 47 citations in OpenAlex.
- Probing amikacin interaction with albumin: A combined multispectral and molecular docking investigation.Heliyon · 2024Article
- Identification, screening, and comprehensive evaluation of novel thrombin inhibitory peptides from the hirudo produced using pepsin.Frontiers in pharmacology · 2024Article
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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
- Synthesis, substitution kinetics, DNA/BSA binding and cytotoxicity of tridentate N^E^N (E = NH, O, S) pyrazolyl palladium(II) complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Article
- Heme Protein Binding of Sulfonamide Compounds: A Correlation Study by Spectroscopic, Calorimetric, and Computational Methods.ACS omega · 2022Article
- Article
- α-Glucosidase inhibitors from Chinese bayberry (RSC advances · 2020Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binding characteristics of indigotin with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by various spectroscopic techniques. Spectroscopic analysis revealed that the quenching mechanism between indigotin and HSA/BSA belonged to the static quenching. The displacement experiments suggested that indigotin primarily bound to tryptophan residues on proteins within site I. The thermodynamic parameters indicated that the binding of indigotin-HSA/BSA mainly depended on the hydrophobic interaction. The binding distance of indigotin to HSA/BSA was evaluated. The results by synchronous fluorescence, three-dimensional fluorescence, Fourier Transform Infrared spectroscopy (FT-IR) and circular dichroism (CD) spectra showed that the conformation of proteins altered in the presence of indigotin.
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