ArticleScientific reports2021
In silico and multi-spectroscopic analyses on the interaction of 5-amino-8-hydroxyquinoline and bovine serum albumin as a potential anticancer agent.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 23 citations in OpenAlex.
- Utilizing Proteolytic-Resistant Nano-Short Peptide Based on Naphthyl Tail-Anchored to Combat Bacterial Infections.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Exploring the binding interaction of 1,4-naphthoquinone derivative-human serum albumin complex by biophysics and molecular simulation.Scientific reports · 2025Article
- Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations.Scientific reports · 2024Article
- Recent Updates on Interaction Studies and Drug Delivery of Antimalarials with Serum Albumin Proteins.Current medicinal chemistry · 2024Review
- Evaluation of phytochemicals of Poria cocos against tyrosinase protein: a virtual screening, pharmacoinformatics and molecular dynamics study.3 Biotech · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
5-Amino-8-hydroxyquinoline (5A8HQ), an amino derivative of 8-hydroxyquinoline, has become a potential anticancer candidate because of its promising proteasome inhibitory activity to overcome and yet synergize bortezomib for fighting cancers. Therefore, in this study, its physicochemical properties and interaction activities with serum protein have extensively been elucidated by both in vitro and in silico approaches to fulfill the pharmacokinetic and pharmacodynamic gaps. 5A8HQ exhibited the drug-likeness properties, where oral administration seems to be a route of choice owing to its high-water solubility and intestinal absorptivity. Multi-spectroscopic investigations suggested that 5A8HQ tended to associate with bovine serum albumin (BSA), a representative of serum protein, via the ground-state complexation. It apparently bound in a protein cleft between subdomains IIA and IIIA of BSA as suggested by the molecular docking and molecular dynamics simulations. The binding was mainly driven by hydrogen bonding and electrostatic interactions with a moderate binding constant at 10
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