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

Del Giudice, Alessandra; Dicko, Cedric LU ; Galantini, Luciano and Pavel, Nicolae V. (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).

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author
organization
publishing date
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
external identifiers
  • scopus:85016952640
  • wos:000389622600004
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
2017-09-18 13:34:17
@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 &lt;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},
  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},
  volume       = {120},
  year         = {2016},
}