Title : Sulfate anion delays the self-assembly of human insulin by modifying the aggregation pathway.

Pub. Date : 2014 Jul 1

PMID : 24988354






3 Functional Relationships(s)
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1 In this work, we characterize the aggregation process of human insulin at acidic pH in the presence of sulfate ions using a combination of Thioflavin T fluorescence, dynamic light scattering, size exclusion chromatography, Fourier transform infrared spectroscopy, and transmission electron microscopy. Sulfates insulin Homo sapiens
2 It is found that the increase of sulfate concentration inhibits the conversion of insulin molecules into aggregates by modifying the aggregation pathway. Sulfates insulin Homo sapiens
3 When the sulfate concentration is increased above 5 mM, the sulfate anion induces the salting-out of ~18-20% of insulin molecules into reversible amorphous aggregates, which retain a large content of alpha-helix structures. Sulfates insulin Homo sapiens