Structural response of human serum albumin to oxidation: Biological buffer to local formation of hypochlorite

Research output: Contribution to journalArticle


The most abundant plasma protein, human serum albumin (HSA), plays a key part in the body's antioxidant defense against reactive species. This study was aimed at correlating oxidant-induced chemical and structural effects on HSA. Despite the chemical modification induced by the oxidant hypochlorite, the native shape is preserved up to oxidant/HSA molar ratio <80, above which a structural transition occurs in the critical range 80-120. This conformational variation involves the drifting of one of the end-domains from the rest of the protein and corresponds to the loss of one-third of the α-helix and a net increase of the protein negative charge. The transition is highly reproducible suggesting that it represents a well-defined structural response typical of this multidomain protein. The ability to tolerate high levels of chemical modification in a folded or only partially unfolded state, as well as the stability to aggregation, provides albumin with optimal features as a biological buffer for the local formation of oxidants. (Graph Presented).


  • Alessandra Del Giudice
  • Cedric Dicko
  • Luciano Galantini
  • Nicolae V. Pavel
External organisations
  • Sapienza University of Rome
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biochemistry and Molecular Biology
Original languageEnglish
Pages (from-to)12261-12271
Number of pages11
JournalJournal of Physical Chemistry B
Issue number40
Publication statusPublished - 2016 Nov 10
Publication categoryResearch