http://www.cnr.it/ontology/cnr/individuo/prodotto/ID286645
Cigarette smoke induces alterations in the drug binding properties of human serum albumin (Articolo in rivista)
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- Label
- Cigarette smoke induces alterations in the drug binding properties of human serum albumin (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bcmd.2014.04.009 (literal)
- Alternative label
Clerici M.; Colombo G.; Secundo F.; Gagliano N.; Colombo R.; Portinaro N.; Giustarini D.; Milzani A.; Rossi R.; Dalle-Donne I. (2014)
Cigarette smoke induces alterations in the drug binding properties of human serum albumin
in Blood cells, molecules, & diseases (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Clerici M.; Colombo G.; Secundo F.; Gagliano N.; Colombo R.; Portinaro N.; Giustarini D.; Milzani A.; Rossi R.; Dalle-Donne I. (literal)
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- http://www.scopus.com/inward/record.url?eid=2-s2.0-84904762547&partnerID=q2rCbXpz (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- Department of Biosciences, Università degli Studi di Milano, Milan, Italy; Department of Life Sciences, University of Siena, Siena, Italy; Department of Biomedical Sciences for Health, Università degli Studi di Milano, Milan, Italy; Department of Medical Biotechnology and Translational Medicine, Clinica Ortopedica e Traumatologica, Università degli Studi di Milano, and Istituto Clinico Humanitas, Rozzano, Milan, Italy; Istituto di Chimica del Riconoscimento Molecolare, CNR, Milan, Italy (literal)
- Titolo
- Cigarette smoke induces alterations in the drug binding properties of human serum albumin (literal)
- Abstract
- Albumin is the most abundant plasma protein and serves as a transport and depot protein for numerous endogenous and exogenous compounds. Earlier we had shown that cigarette smoke induces carbonylation of human serum albumin (HSA) and alters its redox state. Here, the effect of whole-phase cigarette smoke on HSA ligand binding properties was evaluated by equilibrium dialysis and size-exclusion HPLC or tryptophan fluorescence. The binding of salicylic acid and naproxen to cigarette smoke-oxidized HSA resulted to be impaired, unlike that of curcumin and genistein, chosen as representative ligands. The binding of the hydrophobic fluorescent probe 4,4'-bis(1-anilino-8-naphtalenesulfonic acid) (bis-ANS), intrinsic tryptophan fluorescence, and susceptibility to enzymatic proteolysis revealed slight changes in albumin conformation. These findings suggest that cigarette smoke-induced modifications of HSA may affect the binding, transport and bioavailability of specific ligands in smokers. © 2014 Elsevier Inc. (literal)
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