Influence of metal ions on thermal aggregation of bovine serum albumin:Aggregation kinetics and structural changes

Maurizio Leone, Valeria Militello, Giovanna Navarra, Armida Torreggiani, Anna Tinti

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Abstract

Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies. Inthis work the effects of Cu(II) and Zn(II) ions on heat-induced structural modifications of bovine serumalbumin (BSA) were studied, with the aim of delineating the role of these ions in the early stages of proteinsaggregation kinetics. A joint application of different techniques was used. The aggregate growth wasfollowed by dynamic light scattering measurements, whereas the conformational changes occurring inthe protein structure were monitored by Raman and IR spectroscopy. Both in absence and in presenceof metal ions, heating treatment gave rise to b-structures to the detriment of a-helix conformation ofBSA. The temperature of protein unfolding was not sensitively affected by the presence of Zn(II) or Cu(II)ions; on the contrary, only Zn(II) ions slightly promoted the heat-induced aggregation of the protein,since bigger aggregates were formed in their presence. The different efficacy of the Cu(II) and Zn(II) ionsin promoting the BSA aggregation were highlighted by Raman measurements, assessing the role of Hisresidues in metal binding. A distinct polypeptide folding of the two metal–BSA systems takes place, sincethe predominant mode of metal binding depends on metal. In particular, in Zn–BSA the metal coordinationinvolves the imidazole Ns atom of His which can promote inter-molecular cross-linking.2009 Elsevier Inc. All rights reserved.
Lingua originaleEnglish
pagine (da-a)1729-1738
Numero di pagine10
RivistaDefault journal
Volume103
Stato di pubblicazionePublished - 2009

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Bovine Serum Albumin
Metal ions
Agglomeration
Hot Temperature
Metals
Ions
Kinetics
Proteins
Pathology
Dynamic light scattering
Protein Unfolding
Raman spectroscopy
Conformations
Infrared spectroscopy
Raman Spectrum Analysis
Heating
Atoms
Peptides
Temperature
Growth

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

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title = "Influence of metal ions on thermal aggregation of bovine serum albumin:Aggregation kinetics and structural changes",
abstract = "Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies. Inthis work the effects of Cu(II) and Zn(II) ions on heat-induced structural modifications of bovine serumalbumin (BSA) were studied, with the aim of delineating the role of these ions in the early stages of proteinsaggregation kinetics. A joint application of different techniques was used. The aggregate growth wasfollowed by dynamic light scattering measurements, whereas the conformational changes occurring inthe protein structure were monitored by Raman and IR spectroscopy. Both in absence and in presenceof metal ions, heating treatment gave rise to b-structures to the detriment of a-helix conformation ofBSA. The temperature of protein unfolding was not sensitively affected by the presence of Zn(II) or Cu(II)ions; on the contrary, only Zn(II) ions slightly promoted the heat-induced aggregation of the protein,since bigger aggregates were formed in their presence. The different efficacy of the Cu(II) and Zn(II) ionsin promoting the BSA aggregation were highlighted by Raman measurements, assessing the role of Hisresidues in metal binding. A distinct polypeptide folding of the two metal–BSA systems takes place, sincethe predominant mode of metal binding depends on metal. In particular, in Zn–BSA the metal coordinationinvolves the imidazole Ns atom of His which can promote inter-molecular cross-linking.2009 Elsevier Inc. All rights reserved.",
keywords = "Bovine Serum Albumin; Raman Spectroscopy, Infrared Spectroscopy; Thermal aggregation; Copper and Zinc ions",
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TY - JOUR

T1 - Influence of metal ions on thermal aggregation of bovine serum albumin:Aggregation kinetics and structural changes

AU - Leone, Maurizio

AU - Militello, Valeria

AU - Navarra, Giovanna

AU - Torreggiani, Armida

AU - Tinti, Anna

PY - 2009

Y1 - 2009

N2 - Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies. Inthis work the effects of Cu(II) and Zn(II) ions on heat-induced structural modifications of bovine serumalbumin (BSA) were studied, with the aim of delineating the role of these ions in the early stages of proteinsaggregation kinetics. A joint application of different techniques was used. The aggregate growth wasfollowed by dynamic light scattering measurements, whereas the conformational changes occurring inthe protein structure were monitored by Raman and IR spectroscopy. Both in absence and in presenceof metal ions, heating treatment gave rise to b-structures to the detriment of a-helix conformation ofBSA. The temperature of protein unfolding was not sensitively affected by the presence of Zn(II) or Cu(II)ions; on the contrary, only Zn(II) ions slightly promoted the heat-induced aggregation of the protein,since bigger aggregates were formed in their presence. The different efficacy of the Cu(II) and Zn(II) ionsin promoting the BSA aggregation were highlighted by Raman measurements, assessing the role of Hisresidues in metal binding. A distinct polypeptide folding of the two metal–BSA systems takes place, sincethe predominant mode of metal binding depends on metal. In particular, in Zn–BSA the metal coordinationinvolves the imidazole Ns atom of His which can promote inter-molecular cross-linking.2009 Elsevier Inc. All rights reserved.

AB - Metal ions are implicated in protein aggregation processes of several neurodegenerative pathologies. Inthis work the effects of Cu(II) and Zn(II) ions on heat-induced structural modifications of bovine serumalbumin (BSA) were studied, with the aim of delineating the role of these ions in the early stages of proteinsaggregation kinetics. A joint application of different techniques was used. The aggregate growth wasfollowed by dynamic light scattering measurements, whereas the conformational changes occurring inthe protein structure were monitored by Raman and IR spectroscopy. Both in absence and in presenceof metal ions, heating treatment gave rise to b-structures to the detriment of a-helix conformation ofBSA. The temperature of protein unfolding was not sensitively affected by the presence of Zn(II) or Cu(II)ions; on the contrary, only Zn(II) ions slightly promoted the heat-induced aggregation of the protein,since bigger aggregates were formed in their presence. The different efficacy of the Cu(II) and Zn(II) ionsin promoting the BSA aggregation were highlighted by Raman measurements, assessing the role of Hisresidues in metal binding. A distinct polypeptide folding of the two metal–BSA systems takes place, sincethe predominant mode of metal binding depends on metal. In particular, in Zn–BSA the metal coordinationinvolves the imidazole Ns atom of His which can promote inter-molecular cross-linking.2009 Elsevier Inc. All rights reserved.

KW - Bovine Serum Albumin; Raman Spectroscopy

KW - Infrared Spectroscopy; Thermal aggregation; Copper and Zinc ions

UR - http://hdl.handle.net/10447/40921

M3 - Article

VL - 103

SP - 1729

EP - 1738

JO - Default journal

JF - Default journal

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