Publication: In silico and multi-spectroscopic analyses on the interaction of 5-amino-8-hydroxyquinoline and bovine serum albumin as a potential anticancer agent
Issued Date
2021-12-01
Resource Type
ISSN
20452322
Other identifier(s)
2-s2.0-85117422080
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Scientific Reports. Vol.11, No.1 (2021)
Suggested Citation
Waralee Ruankham, Kamonrat Phopin, Ratchanok Pingaew, Supaluk Prachayasittikul, Virapong Prachayasittikul, Tanawut Tantimongcolwat In silico and multi-spectroscopic analyses on the interaction of 5-amino-8-hydroxyquinoline and bovine serum albumin as a potential anticancer agent. Scientific Reports. Vol.11, No.1 (2021). doi:10.1038/s41598-021-99690-2 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/79206
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
In silico and multi-spectroscopic analyses on the interaction of 5-amino-8-hydroxyquinoline and bovine serum albumin as a potential anticancer agent
Other Contributor(s)
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 104 M−1, conforming with the predicted free fraction in serum at 0.484. Therefore, 5A8HQ seems to display a good bioavailability in plasma to reach target sites and exerts its potent pharmacological activity. Likewise, serum albumin is a good candidate to be reservoir and transporter of 5A8HQ in the circulatory system.