Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/17321
ชื่อเรื่อง: In silico and multi-spectroscopic analyses on the interaction of 5-amino-8-hydroxyquinoline and bovine serum albumin as a potential anticancer agent
ผู้แต่ง: Ruankham W.
Phopin K.
Pingaew R.
Prachayasittikul S.
Prachayasittikul V.
Tantimongcolwat T.
Keywords: 5-amino-8-hydroxyquinoline
antineoplastic agent
bovine serum albumin
protein binding
quinolinol derivative
animal
binding site
bovine
chemical structure
chemistry
circular dichroism
human
metabolism
molecular docking
molecular dynamics
protein conformation
spectrofluorometry
thermodynamics
ultraviolet spectrophotometry
Animals
Antineoplastic Agents
Binding Sites
Cattle
Circular Dichroism
Humans
Hydroxyquinolines
Molecular Docking Simulation
Molecular Dynamics Simulation
Molecular Structure
Protein Binding
Protein Conformation
Serum Albumin, Bovine
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Thermodynamics
วันที่เผยแพร่: 2021
บทคัดย่อ: 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. © 2021, The Author(s).
URI: https://ir.swu.ac.th/jspui/handle/123456789/17321
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85117422080&doi=10.1038%2fs41598-021-99690-2&partnerID=40&md5=37d6bbc10b12988d9801172e7438114b
ISSN: 20452322
Appears in Collections:Scopus 1983-2021

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