Locating the binding sites of Pb(II) ion with human and bovine serum albumins.

Lead is a potent environmental toxin that has accumulated above its natural level as a result of human activity. Pb cation shows major affinity towards protein complexation and it has been used as modulator of protein-membrane interactions. We located the binding sites of Pb(II) with human serum (HS...

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Autores principales:	Ahmed Belatik, Surat Hotchandani, Robert Carpentier, Heidar-Ali Tajmir-Riahi
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8ea4b7b7a3034c288eee3dd9f075be29
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spelling	oai:doaj.org-article:8ea4b7b7a3034c288eee3dd9f075be292021-11-18T07:19:32ZLocating the binding sites of Pb(II) ion with human and bovine serum albumins.1932-620310.1371/journal.pone.0036723https://doaj.org/article/8ea4b7b7a3034c288eee3dd9f075be292012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22574219/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Lead is a potent environmental toxin that has accumulated above its natural level as a result of human activity. Pb cation shows major affinity towards protein complexation and it has been used as modulator of protein-membrane interactions. We located the binding sites of Pb(II) with human serum (HSA) and bovine serum albumins (BSA) at physiological conditions, using constant protein concentration and various Pb contents. FTIR, UV-visible, CD, fluorescence and X-ray photoelectron spectroscopic (XPS) methods were used to analyse Pb binding sites, the binding constant and the effect of metal ion complexation on HSA and BSA stability and conformations. Structural analysis showed that Pb binds strongly to HSA and BSA via hydrophilic contacts with overall binding constants of K(Pb-HSA) = 8.2 (±0.8)×10(4) M(-1) and K(Pb-BSA) = 7.5 (±0.7)×10(4) M(-1). The number of bound Pb cation per protein is 0.7 per HSA and BSA complexes. XPS located the binding sites of Pb cation with protein N and O atoms. Pb complexation alters protein conformation by a major reduction of α-helix from 57% (free HSA) to 48% (metal-complex) and 63% (free BSA) to 52% (metal-complex) inducing a partial protein destabilization.Ahmed BelatikSurat HotchandaniRobert CarpentierHeidar-Ali Tajmir-RiahiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 5, p e36723 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ahmed Belatik Surat Hotchandani Robert Carpentier Heidar-Ali Tajmir-Riahi Locating the binding sites of Pb(II) ion with human and bovine serum albumins.
description	Lead is a potent environmental toxin that has accumulated above its natural level as a result of human activity. Pb cation shows major affinity towards protein complexation and it has been used as modulator of protein-membrane interactions. We located the binding sites of Pb(II) with human serum (HSA) and bovine serum albumins (BSA) at physiological conditions, using constant protein concentration and various Pb contents. FTIR, UV-visible, CD, fluorescence and X-ray photoelectron spectroscopic (XPS) methods were used to analyse Pb binding sites, the binding constant and the effect of metal ion complexation on HSA and BSA stability and conformations. Structural analysis showed that Pb binds strongly to HSA and BSA via hydrophilic contacts with overall binding constants of K(Pb-HSA) = 8.2 (±0.8)×10(4) M(-1) and K(Pb-BSA) = 7.5 (±0.7)×10(4) M(-1). The number of bound Pb cation per protein is 0.7 per HSA and BSA complexes. XPS located the binding sites of Pb cation with protein N and O atoms. Pb complexation alters protein conformation by a major reduction of α-helix from 57% (free HSA) to 48% (metal-complex) and 63% (free BSA) to 52% (metal-complex) inducing a partial protein destabilization.
format	article
author	Ahmed Belatik Surat Hotchandani Robert Carpentier Heidar-Ali Tajmir-Riahi
author_facet	Ahmed Belatik Surat Hotchandani Robert Carpentier Heidar-Ali Tajmir-Riahi
author_sort	Ahmed Belatik
title	Locating the binding sites of Pb(II) ion with human and bovine serum albumins.
title_short	Locating the binding sites of Pb(II) ion with human and bovine serum albumins.
title_full	Locating the binding sites of Pb(II) ion with human and bovine serum albumins.
title_fullStr	Locating the binding sites of Pb(II) ion with human and bovine serum albumins.
title_full_unstemmed	Locating the binding sites of Pb(II) ion with human and bovine serum albumins.
title_sort	locating the binding sites of pb(ii) ion with human and bovine serum albumins.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/8ea4b7b7a3034c288eee3dd9f075be29
work_keys_str_mv	AT ahmedbelatik locatingthebindingsitesofpbiiionwithhumanandbovineserumalbumins AT surathotchandani locatingthebindingsitesofpbiiionwithhumanandbovineserumalbumins AT robertcarpentier locatingthebindingsitesofpbiiionwithhumanandbovineserumalbumins AT heidaralitajmirriahi locatingthebindingsitesofpbiiionwithhumanandbovineserumalbumins
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Locating the binding sites of Pb(II) ion with human and bovine serum albumins.

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