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 alpha-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.

Structural response of human serum albumin to oxidation: bological buffer to local formation of hypochlorite / DEL GIUDICE, Alessandra; Dicko, Cedric; Galantini, Luciano; Pavel, Nicolae Viorel. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - STAMPA. - 120:48(2016), pp. 12261-12271. [10.1021/acs.jpcb.6b08601]

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

DEL GIUDICE, ALESSANDRA
;
GALANTINI, Luciano;PAVEL, Nicolae Viorel
2016

Abstract

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 alpha-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.
2016
protein oxidation; albumin; hypochlorite; small-angle X-ray scattering
01 Pubblicazione su rivista::01a Articolo in rivista
Structural response of human serum albumin to oxidation: bological buffer to local formation of hypochlorite / DEL GIUDICE, Alessandra; Dicko, Cedric; Galantini, Luciano; Pavel, Nicolae Viorel. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - STAMPA. - 120:48(2016), pp. 12261-12271. [10.1021/acs.jpcb.6b08601]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/929726
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