Fibrillar beta-lactoglobulin gels: Part 1. Fibril formation and structure

Walraj S Gosal, Allan H Clark, Simon B Ross-Murphy

Research output: Contribution to journalArticlepeer-review

155 Citations (Scopus)

Abstract

As a prelude to experimental and theoretical work on the mechanical properties of fibrillar beta-lactoglobulin gels, this paper reports the structural characterization of beta-lactoglobulin fibrils by electron and atomic force microscopy (AFM), infrared and Raman spectroscopy, and powder X-ray diffraction. Aggregates formed by incubation of beta-lactoglobulin in various alcohol-water mixtures at pH 2, and in water-trifluoroethanol (TFE) at pH 7, were found to be wormlike (approximately 7 nm in width and 1 microm in length), smoother, and seemingly stiffer fibrils formed on heating aqueous beta-lactoglobulin solutions at pH 2 and low ionic strength, although there was little evidence for the higher-order structures common in most amyloid-forming systems. Time-lapse AFM also revealed differences in the formation of these two fibril types: thermally induced aggregation occurring more cooperatively, in keeping with a nucleation and growth process. Only short stiff-rods (
Original languageEnglish
Pages (from-to)2408-19
Number of pages12
JournalBiomacromolecules
Volume5
Issue number6
DOIs
Publication statusPublished - 2004

Keywords

  • Amyloid
  • Animals
  • Biocompatible Materials
  • Cattle
  • Gels
  • Hydrogen-Ion Concentration
  • Insulin
  • Ions
  • Lactoglobulins
  • Macromolecular Substances
  • Magnetic Resonance Spectroscopy
  • Microscopy, Atomic Force
  • Microscopy, Electron
  • Milk
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Solvents
  • Spectroscopy, Fourier Transform Infrared
  • Spectrum Analysis, Raman
  • Temperature
  • Time Factors
  • Water
  • X-Ray Diffraction

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