Study of the binding equilibrium between Zn(II) and HSA by capillary electrophoresis–inductively coupled plasma optical emission spectrometry

Deng, Biyang; Wang, Yingzi; Zhu, Peng; Xu, Xiangshu; Xi, Ning

doi:10.1016/j.aca.2010.10.018

Cited by 30 publications

(19 citation statements)

References 44 publications

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“…Zinc is believed to be chelated by imidazole at histidine residues, but some non-specific binding could also involve cysteine residues [63,64]. Regarding copper ions, serum albumin has one strong binding site in the N-terminal tripeptide (Asp-Ala-His) for Cu(II), but histidine residues are also suggested as a major ligand, similarly to cysteine [35].…”

Section: Discussionmentioning

confidence: 99%

Deciphering metal-induced oxidative damages on glycated albumin structure and function

Baraka-Vidot¹,

Navarra

Leone

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background: Metal ions such as copper or zinc are involved in the development of neurodegenerative pathologies and metabolic diseases such as diabetes mellitus. Albumin structure and functions are impaired following metaland glucose-mediated oxidative alterations. The aim of this study was to elucidate effects of Cu(II) and Zn(II) ions on glucose-induced modifications in albumin by focusing on glycation, aggregation, oxidation and functional aspects. Methods: Aggregation and conformational changes in albumin were monitored by spectroscopy, fluorescence and microscopy techniques. Biochemical assays such as carbonyl, thiol groups, albumin-bound Cu, fructosamine and amine group measurements were used. Cellular assays were used to gain functional information concerning antioxidant activity of oxidized albumins. Results: Both metals promoted inhibition of albumin glycation associated with an enhanced aggregation and oxidation process. Metal ions gave rise to the formation of β-amyloid type aggregates in albumin exhibiting impaired antioxidant properties and toxic activity to murine microglia cells (BV2). The differential efficiency of both metal ions to inhibit albumin glycation, to promote aggregation and to affect cellular physiology is compared. Conclusions and general significance: Considering the key role of oxidized protein in pathology complications, glycation-mediated and metal ion-induced impairment of albumin properties might be important parameters to be followed and fought.

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Section: Discussionmentioning

confidence: 99%

Deciphering metal-induced oxidative damages on glycated albumin structure and function

Baraka-Vidot¹,

Navarra

Leone

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…HSA displays a wide variety of binding sites for several metal ions, including Mg(II), Al(III), Ca(II), Mn(II), Co(II/III), Ni(II), Cu(I/II), Zn(II), Cd(II), Pt(II), Au(I/II), Hg(II), and Tb(III) (Peters, 1996Sokołowska et al, 2009Deng et al, 2010;Duff and Kumar, 2009). So far, three major binding sites endowed with appropriate residues matching for the different metal geometries have been observed.…”

Section: Metal Binding Sitesmentioning

confidence: 99%

Human serum albumin: From bench to bedside

Fanali

Masi

Trezza

et al. 2012

Molecular Aspects of Medicine

1,515

1,452

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“…In particular, serum albumin is the major soluble protein constituent of the circulatory system, its concentration ranging between 3.5% and 5% in plasma, and up to 4% in inflammatory exudate; binding of metals by serum albumin has been described to form stable metal ion-bovine serum albumin (BSA) complexes [17][18][19]. Recently, Zhao et al.…”

Section: Introductionmentioning

confidence: 99%