Conformational changes involved in thermal aggregation processes of bovine serum albumin

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Abstract

We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circular dichroism measurements. These data contribute to clarify the connection between conformational changes at tertiary and secondary structure level during the aggregation and how the different domains are involved. We also discuss the relevant role played by cysteine 34 in the aggregation pathways. © 2003 Elsevier B.V. All rights reserved.
Lingua originaleEnglish
pagine (da-a)133-141
Numero di pagine9
RivistaBiophysical Chemistry
Volume105
Stato di pubblicazionePublished - 2003

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Bovine Serum Albumin
Cysteine
Agglomeration
Hot Temperature
Circular Dichroism
Tryptophan
Coloring Agents
Fluorescence
Rayleigh scattering
Dichroism
Proteins
Kinetics
fluorescein 5-maleimide

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Organic Chemistry

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title = "Conformational changes involved in thermal aggregation processes of bovine serum albumin",
abstract = "We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circular dichroism measurements. These data contribute to clarify the connection between conformational changes at tertiary and secondary structure level during the aggregation and how the different domains are involved. We also discuss the relevant role played by cysteine 34 in the aggregation pathways. {\circledC} 2003 Elsevier B.V. All rights reserved.",
keywords = "Biochemistry, Biophysics, Bovine serum albumin, Circular dichroism, Conformational changes, Physical and Theoretical Chemistry, Protein aggregation, Steady-state fluorescence",
author = "Valeria Militello and Maurizio Leone and Valeria Vetri",
year = "2003",
language = "English",
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journal = "Biophysical Chemistry",
issn = "0301-4622",
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TY - JOUR

T1 - Conformational changes involved in thermal aggregation processes of bovine serum albumin

AU - Militello, Valeria

AU - Leone, Maurizio

AU - Vetri, Valeria

PY - 2003

Y1 - 2003

N2 - We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circular dichroism measurements. These data contribute to clarify the connection between conformational changes at tertiary and secondary structure level during the aggregation and how the different domains are involved. We also discuss the relevant role played by cysteine 34 in the aggregation pathways. © 2003 Elsevier B.V. All rights reserved.

AB - We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circular dichroism measurements. These data contribute to clarify the connection between conformational changes at tertiary and secondary structure level during the aggregation and how the different domains are involved. We also discuss the relevant role played by cysteine 34 in the aggregation pathways. © 2003 Elsevier B.V. All rights reserved.

KW - Biochemistry

KW - Biophysics

KW - Bovine serum albumin

KW - Circular dichroism

KW - Conformational changes

KW - Physical and Theoretical Chemistry

KW - Protein aggregation

KW - Steady-state fluorescence

UR - http://hdl.handle.net/10447/129522

M3 - Article

VL - 105

SP - 133

EP - 141

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

ER -