Cigarette smoke induces alterations in the drug binding properties of human serum albumin

Marco Clerici, Graziano Colombo, Francesco Secundo, Nicoletta Gagliano, Roberto Colombo, Nicola Portinaro, Daniela Giustarini, Aldo Milzani, Ranieri Rossi, Isabella Dalle-Donne

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)149-156
Number of pages8
JournalBlood cells, molecules & diseases
Volume53
Issue number3
DOIs
Publication statusPublished - 2014

Keywords

  • Cigarette smoke
  • Human serum albumin
  • Naproxen
  • Oxidation
  • Protein conformation
  • Salicylic acid

ASJC Scopus subject areas

  • Molecular Biology
  • Molecular Medicine
  • Hematology
  • Cell Biology

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  • Cite this

    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. Blood cells, molecules & diseases, 53(3), 149-156. https://doi.org/10.1016/j.bcmd.2014.04.009