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Updated: Jul 27, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
alpha-L-iduronidase forms semi-crystalline spherulites with amyloid-like properties
L Ruth1, D Eisenberg, E F Neufeld
1Department of Biological Chemistry and Molecular Biology Institute, University California Los Angeles, Los Angeles, CA 90095, USA.
Abstract:
While seeking conditions for single crystals of human alpha-L-iduronidase, solutions were discovered (pH 3.0-8.5 containing calcium or zinc salts) that transform soluble alpha-L-iduronidase to a solid aggregate. This aggregate is a spherulite of semi-crystalline protein. The X-ray diffraction pattern and ability to bind Congo red characterize the alpha-L-iduronidase spherulite as 'amyloid-like', in that it displays two of the characteristics of amyloidogenic proteins. In addition, alpha-L-iduronidase also interacts with heparin, as do some amyloid-forming proteins.
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