Structural response of human serum albumin to oxidation : Biological buffer to local formation of hypochlorite
(2016) In Journal of Physical Chemistry B 120(40). p.12261-12271- 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 α-helix and a net increase of the protein negative charge. The transition is highly reproducible suggesting that it represents a well-defined... (More)
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).
(Less)
- author
- Del Giudice, Alessandra ; Dicko, Cedric LU ; Galantini, Luciano and Pavel, Nicolae V.
- organization
- publishing date
- 2016-11-10
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Physical Chemistry B
- volume
- 120
- issue
- 40
- pages
- 11 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:27934228
- wos:000389622600004
- scopus:85016952640
- ISSN
- 1520-6106
- DOI
- 10.1021/acs.jpcb.6b08601
- language
- English
- LU publication?
- yes
- id
- 5219c239-e7c1-4571-9929-f3bdf302b39d
- date added to LUP
- 2017-05-05 15:31:52
- date last changed
- 2024-06-23 16:33:10
@article{5219c239-e7c1-4571-9929-f3bdf302b39d, abstract = {{<p>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).</p>}}, author = {{Del Giudice, Alessandra and Dicko, Cedric and Galantini, Luciano and Pavel, Nicolae V.}}, issn = {{1520-6106}}, language = {{eng}}, month = {{11}}, number = {{40}}, pages = {{12261--12271}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Journal of Physical Chemistry B}}, title = {{Structural response of human serum albumin to oxidation : Biological buffer to local formation of hypochlorite}}, url = {{http://dx.doi.org/10.1021/acs.jpcb.6b08601}}, doi = {{10.1021/acs.jpcb.6b08601}}, volume = {{120}}, year = {{2016}}, }