Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/11915
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPatnin S.
dc.contributor.authorMakarasen A.
dc.contributor.authorKuno M.
dc.contributor.authorDeeyohe S.
dc.contributor.authorTechasakul S.
dc.contributor.authorChaivisuthangkura A.
dc.date.accessioned2021-04-05T03:01:27Z-
dc.date.available2021-04-05T03:01:27Z-
dc.date.issued2020
dc.identifier.issn13861425
dc.identifier.other2-s2.0-85080072589
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/11915-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85080072589&doi=10.1016%2fj.saa.2020.118159&partnerID=40&md5=eac21d1334486f70d3f29177cd1aec69
dc.description.abstractIn the present investigation, the intermolecular interaction of 4-(4′-cyanophenoxy)-2-(4′′-cyanophenyl)-aminoquinoline (1), a potent non-nucleoside HIV-1 reverse transcriptase inhibitors, with the transport proteins, namely bovine serum albumin (BSA) and human serum albumin (HSA), has been investigated under physiological conditions employing UV–Vis, fluorescence spectrophotometry, competitive binding experiments and molecular docking methods. The results indicated that binding of (1) to the transport proteins caused fluorescence quenching though a static quenching mechanism. The number of binding site (n) and the apparent binding constant (Kb) between (1) and the transport proteins were determined to be about 1 and 104–105 L·mol−1 (at three different temperatures; 298, 308, 318 K), respectively. The interaction of (1) upon binding to the transport proteins was spontaneous. The enthalpic change (ΔH°) and the entropic change (ΔS°) were calculated to be −56.50 kJ·mol−1, −72.31 J·mol−1 K−1 for (1)/BSA, respectively and computed to be −49.35 kJ·mol−1, −58.64 J·mol−1 K−1, respectively for (1)/HSA, respectively. The results implied that the process of interaction force of (1) with the transport protein were Vander Waals force and/or hydrogen bonding interactions. The site maker competitive experiments revealed that the binding site of (1) with the transport proteins were mainly located within site I (sub-domain IIA) in both proteins. Additionally, the molecular docking experiment supported the above results which confirmed the binding interaction between (1) and the transport proteins. This study will come up with basic data for explicating the binding mechanisms of (1) with the transport protein and can be great significance in the opening to clarify the transport process of (1) in vivo. © 2020 Elsevier B.V.
dc.subjectBinding energy
dc.subjectDiseases
dc.subjectFluorescence
dc.subjectFluorescence spectroscopy
dc.subjectHydrogen bonds
dc.subjectMammals
dc.subjectMolecular modeling
dc.subjectQuenching
dc.subjectSpectrophotometry
dc.subjectFluorescence spectrophotometry
dc.subjectHIV-1 reverse transcriptase
dc.subjectHydrogen bonding interactions
dc.subjectIntermolecular interactions
dc.subjectMolecular docking
dc.subjectNNRTIs
dc.subjectSerum albumin
dc.subjectVIS spectrophotometry
dc.subjectProteins
dc.subjectbovine serum albumin
dc.subjecthuman serum albumin
dc.subjectRNA directed DNA polymerase inhibitor
dc.subjectanimal
dc.subjectbinding site
dc.subjectbovine
dc.subjectchemistry
dc.subjecthuman
dc.subjectHuman immunodeficiency virus 1
dc.subjectmolecular docking
dc.subjectultraviolet spectrophotometry
dc.subjectAnimals
dc.subjectBinding Sites
dc.subjectCattle
dc.subjectHIV-1
dc.subjectHumans
dc.subjectMolecular Docking Simulation
dc.subjectReverse Transcriptase Inhibitors
dc.subjectSerum Albumin, Bovine
dc.subjectSerum Albumin, Human
dc.subjectSpectrophotometry, Ultraviolet
dc.titleBinding interaction of potent HIV-1 NNRTIs, amino-oxy-diarylquinoline with the transport protein using spectroscopic and molecular docking
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy. Vol 233, (2020)
dc.identifier.doi10.1016/j.saa.2020.118159
Appears in Collections:Scopus 1983-2021

Files in This Item:
There are no files associated with this item.


Items in SWU repository are protected by copyright, with all rights reserved, unless otherwise indicated.