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Volume 128, 2005
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Aggregation across the length-scales in β-lactoglobulin

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Abstract

The protein β-lactoglobulin (BLG) has been widely studied, in large part because of its importance to the food industry. Following denaturation during heating, under different conditions of pH it has been found to form either particulate (around the isoelectric point at pH 5.1) or fibrillar gels. The nature of the fibrils has recently been suggested to be the same as that identified with amyloid fibrils known for a wide-range of different proteins and implicated in many disease states. We confirm that the BLG fibrils show all the classical signatures of amyloid fibrils. In addition, the fibrils are capable themselves of aggregating further to form large-scale (many microns in size) spherulites. Polarized light microscopy and Environmental scanning electron microscopy (ESEM) have been used to explore the internal structure of these spherulites under conditions in which the solvent has not been dried off. The factors which determine whether or not the spherulites form have also been considered, together with implications for other amyloid-containing systems.

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Publication details

The article was received on 01 Mar 2004, accepted on 20 Apr 2004 and first published on 14 Sep 2004


Article type: Paper
DOI: 10.1039/B403014A
Citation: Faraday Discuss., 2005,128, 13-27
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    Aggregation across the length-scales in β-lactoglobulin

    E. H. C. Bromley, M. R. H. Krebs and A. M. Donald, Faraday Discuss., 2005, 128, 13
    DOI: 10.1039/B403014A

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