Aggregation across the length-scales in β-lactoglobulin (original) (raw)

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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Article information

DOI

https://doi.org/10.1039/B403014A

Article type

Paper

Submitted

01 Mar 2004

Accepted

20 Apr 2004

First published

14 Sep 2004

Download Citation

Faraday Discuss., 2005,128, 13-27

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