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dc.creatorGligorijević, Nikola
dc.creatorŠukalović, Vladimir
dc.creatorMinić, Simeon
dc.creatorMiljuš, Goran
dc.creatorNedić, Olgica
dc.creatorPenezić, Ana
dc.date.accessioned2021-10-18T07:19:14Z
dc.date.available2021-10-18T07:19:14Z
dc.date.issued2021
dc.identifier.issn0352-5139
dc.identifier.urihttps://cherry.chem.bg.ac.rs/handle/123456789/4667
dc.description.abstractThe binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation.
dc.publisherBelgrade : Serbian Chemical Society
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200019/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200026/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200168/RS//
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceJournal of the Serbian Chemical Society
dc.subjectspectral analysis
dc.subjectmolecular docking
dc.subjectprotein-ligand interaction
dc.subjectprotein stability
dc.subjectprotein structure
dc.titlePhysicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches
dc.typearticleen
dc.rights.licenseBY-NC-ND
dcterms.abstractГлигоријевић, Никола; Пенезић, Aна; Недић, Олгица; Миљуш, Горан; Минић, Симеон; Шукаловић, Владимир;
dc.citation.volume86
dc.citation.issue9
dc.citation.spage795
dc.citation.epage807
dc.identifier.wos000692558700002
dc.identifier.doi10.2298/JSC210420041G
dc.citation.rankM23~
dc.type.versionpublishedVersion
dc.identifier.scopus2-s2.0-85114223943
dc.identifier.fulltexthttps://cherry.chem.bg.ac.rs/bitstream/id/28052/Physicochemical_characterisation_of_pub_2021.pdf


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