Tracing nucleation pathways in protein aggregation by using small angle scattering methods

K. Vogtt, N. Javid, E. Alvarez, J. Sefcik, M.-C. Bellissent-Funel

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Heat and alcohol-induced nucleation pathways of the whey protein β-lactoglobulin were investigated using small angle neutron and X-ray scattering for structural characterization. Protein solutions at various concentrations were either heated stepwise to 80 °C or mixed with ethanol to 50% (v/v). Heating induces dissociation of the β-lactoglobulin dimer in neutral pH aqueous medium, leading to nucleation at about 75 °C of tetrameric, cylindrical clusters, as indicated by three dimensional rigid body and bead modelling performed to fit scattering curves. In contrast to heating, ethanol addition induces the formation of fairly compact, internally disordered sphere-like clusters composed of rod-like submolecular structural units. At higher concentrations these clusters show typical colloidal behaviour, exhibiting long-range repulsive interactions, as also confirmed by dynamic light scattering measurements. The results contrast the effect of different unfolding scenarios on preferred nucleation pathways in subsequent protein assembly processes in various solution environments.
LanguageEnglish
Pages3906-3914
Number of pages9
JournalSoft Matter
Volume7
Issue number8
Early online date28 Feb 2011
DOIs
Publication statusPublished - 21 Apr 2011

Fingerprint

tracing
Lactoglobulins
Nucleation
Agglomeration
nucleation
Scattering
proteins
ethyl alcohol
Ethanol
scattering
Heating
Proteins
heating
Dynamic light scattering
rigid structures
X ray scattering
beads
Dimers
Neutrons
alcohols

Keywords

  • tracing nucleation pathways
  • protein aggregation
  • small angle
  • scattering methods
  • bionanotechnology

Cite this

Vogtt, K. ; Javid, N. ; Alvarez, E. ; Sefcik, J. ; Bellissent-Funel, M.-C. / Tracing nucleation pathways in protein aggregation by using small angle scattering methods. In: Soft Matter. 2011 ; Vol. 7, No. 8. pp. 3906-3914.
@article{19219ae56da249f98b5404478228444f,
title = "Tracing nucleation pathways in protein aggregation by using small angle scattering methods",
abstract = "Heat and alcohol-induced nucleation pathways of the whey protein β-lactoglobulin were investigated using small angle neutron and X-ray scattering for structural characterization. Protein solutions at various concentrations were either heated stepwise to 80 °C or mixed with ethanol to 50{\%} (v/v). Heating induces dissociation of the β-lactoglobulin dimer in neutral pH aqueous medium, leading to nucleation at about 75 °C of tetrameric, cylindrical clusters, as indicated by three dimensional rigid body and bead modelling performed to fit scattering curves. In contrast to heating, ethanol addition induces the formation of fairly compact, internally disordered sphere-like clusters composed of rod-like submolecular structural units. At higher concentrations these clusters show typical colloidal behaviour, exhibiting long-range repulsive interactions, as also confirmed by dynamic light scattering measurements. The results contrast the effect of different unfolding scenarios on preferred nucleation pathways in subsequent protein assembly processes in various solution environments.",
keywords = "tracing nucleation pathways, protein aggregation, small angle, scattering methods, bionanotechnology",
author = "K. Vogtt and N. Javid and E. Alvarez and J. Sefcik and M.-C. Bellissent-Funel",
year = "2011",
month = "4",
day = "21",
doi = "10.1039/c0sm00978d",
language = "English",
volume = "7",
pages = "3906--3914",
journal = "Soft Matter",
issn = "1744-683X",
number = "8",

}

Tracing nucleation pathways in protein aggregation by using small angle scattering methods. / Vogtt, K.; Javid, N.; Alvarez, E.; Sefcik, J.; Bellissent-Funel, M.-C.

In: Soft Matter, Vol. 7, No. 8, 21.04.2011, p. 3906-3914.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Tracing nucleation pathways in protein aggregation by using small angle scattering methods

AU - Vogtt, K.

AU - Javid, N.

AU - Alvarez, E.

AU - Sefcik, J.

AU - Bellissent-Funel, M.-C.

PY - 2011/4/21

Y1 - 2011/4/21

N2 - Heat and alcohol-induced nucleation pathways of the whey protein β-lactoglobulin were investigated using small angle neutron and X-ray scattering for structural characterization. Protein solutions at various concentrations were either heated stepwise to 80 °C or mixed with ethanol to 50% (v/v). Heating induces dissociation of the β-lactoglobulin dimer in neutral pH aqueous medium, leading to nucleation at about 75 °C of tetrameric, cylindrical clusters, as indicated by three dimensional rigid body and bead modelling performed to fit scattering curves. In contrast to heating, ethanol addition induces the formation of fairly compact, internally disordered sphere-like clusters composed of rod-like submolecular structural units. At higher concentrations these clusters show typical colloidal behaviour, exhibiting long-range repulsive interactions, as also confirmed by dynamic light scattering measurements. The results contrast the effect of different unfolding scenarios on preferred nucleation pathways in subsequent protein assembly processes in various solution environments.

AB - Heat and alcohol-induced nucleation pathways of the whey protein β-lactoglobulin were investigated using small angle neutron and X-ray scattering for structural characterization. Protein solutions at various concentrations were either heated stepwise to 80 °C or mixed with ethanol to 50% (v/v). Heating induces dissociation of the β-lactoglobulin dimer in neutral pH aqueous medium, leading to nucleation at about 75 °C of tetrameric, cylindrical clusters, as indicated by three dimensional rigid body and bead modelling performed to fit scattering curves. In contrast to heating, ethanol addition induces the formation of fairly compact, internally disordered sphere-like clusters composed of rod-like submolecular structural units. At higher concentrations these clusters show typical colloidal behaviour, exhibiting long-range repulsive interactions, as also confirmed by dynamic light scattering measurements. The results contrast the effect of different unfolding scenarios on preferred nucleation pathways in subsequent protein assembly processes in various solution environments.

KW - tracing nucleation pathways

KW - protein aggregation

KW - small angle

KW - scattering methods

KW - bionanotechnology

UR - http://www.scopus.com/inward/record.url?scp=79953734305&partnerID=8YFLogxK

U2 - 10.1039/c0sm00978d

DO - 10.1039/c0sm00978d

M3 - Article

VL - 7

SP - 3906

EP - 3914

JO - Soft Matter

T2 - Soft Matter

JF - Soft Matter

SN - 1744-683X

IS - 8

ER -