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

Gosal, Walraj S, Clark, Allan H and Ross-Murphy, Simon B (2004) Fibrillar beta-lactoglobulin gels:Part 1. Fibril formation and structure. Biomacromolecules, 5 (6). pp. 2408-19. ISSN 1525-7797

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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 (

Item Type: Article
Uncontrolled 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
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
Depositing User: Pure Connector
Date Deposited: 27 Jan 2014 13:26
Last Modified: 21 Apr 2020 22:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/46111
DOI: 10.1021/bm049659d

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