Show simple item record

dc.creatorAćimović, Jelena M.
dc.creatorStanimirovic, Bojana D.
dc.creatorTodorović, Nina
dc.creatorJovanović, Vesna B.
dc.creatorMandić, Ljuba M.
dc.date.accessioned2019-01-30T17:24:17Z
dc.date.available2019-01-30T17:24:17Z
dc.date.issued2010
dc.identifier.issn0009-2797
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/719
dc.description.abstractMethylglyoxal (MG), a reactive alpha-oxoaldehyde that is produced in higher quantities in diabetes, uremia, oxidative stress, aging and inflammation, reacts with the thiol groups (in addition to the amino and guanidino groups) of proteins. This causes protein modification, formation of advanced glycated end products (AGEs) and cross-linking. Low molecular mass thiols can be used as competitive targets for MG, preventing the reactions mentioned above. Therefore, this paper investigated how the microenvironment of the thiol group in low molecular mass thiols (cysteine, N-acetylcysteine (NAcCys), carboxymethylcysteine (CMC) and glutathione (GSH)) and human serum albumin (HSA) affected the thiol reaction with MG. The SH group reaction course was monitored by H-1-NMR spectroscopy and spectrophotometric quantification. Changes in the HSA molecules were monitored by SDS-PAGE. The microenvironment of the SH group had a major effect on its reactivity and on the product yield. The reactivity of SH groups decreased in the order Cys > GSH > NAcCys. CMC did not react. The percentages of the reacted SH groups in the equilibrium state were almost equal, regardless of the ratio of thiol compound/MG (1:1, 1:2, 1:5): 38.1 +/- 0.9%; 38.2 +/- 0.7% and 39.0 +/- 0.8% for Cys; 26.5 +/- 0.6%; 26.6 +/- 2.6% and 27.4 +/- 2.5% for GSH; 10.8 +/- 0.9%; and 11.2 +/- 0.7% and 12.2 +/- 0.9% for NAcCys, respectively. Our results explain why substances containing alpha-amino-beta-mercapto-ethane as a pharmacophore are successful scavengers of MG. In equilibrium, HSA SH reacted in high percentages both with an insufficient amount and with an excess of MG (55% and 65%, respectively). An analysis of the hydrophobicity of the microenvironment of the SH group on the HSA surface showed that it could contribute to high levels of SH modification, leading to an increase in the scavenging activity of the albumin thiol.en
dc.publisherElsevier Ireland Ltd, Clare
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS//
dc.rightsrestrictedAccess
dc.sourceChemico-Biological Interactions
dc.subjectMethylglyoxalen
dc.subjectLow molecular mass thiolsen
dc.subjectHSAen
dc.subjectThiol group reactivity and microenvironmenten
dc.subjectProtein glycationen
dc.titleInfluence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxalen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractСтанимировиц, Бојана Д.; Јовановиц, Весна Б.; Мандиц, Љуба М.; Aћимовић, Јелена М.; Тодоровић, Нина;
dc.citation.volume188
dc.citation.issue1
dc.citation.spage21
dc.citation.epage30
dc.citation.other188(1): 21-30
dc.citation.rankM22
dc.identifier.pmid20647007
dc.identifier.doi10.1016/j.cbi.2010.07.013
dc.identifier.rcubConv_2557
dc.identifier.scopus2-s2.0-77956169770
dc.identifier.wos000282391400003
dc.type.versionpublishedVersion


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record