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Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain.

ABSTRACT: Amyloid fibrils are associated with sulfated glycosaminoglycans in the extracellular matrix. The presence of sulfated glycosaminoglycans is known to promote amyloid formation in vitro and in vivo, with the sulfate groups playing a role in this process. In order to understand the role that sulfate plays in amyloid formation, we have studied the effect of salts from the Hofmeister series on the protein structure, stability and amyloid formation of an amyloidogenic light chain protein, AL-12. We have been able to show for the first time a direct correlation between protein stability and amyloid formation enhancement by salts from the Hofmeister series, where SO(4)(2-) conferred the most protein stability and enhancement of amyloid formation. Our study emphasizes the importance of the effect of ions in the protein bound water properties and downplays the role of specific interactions between the protein and ions.

SUBMITTER: Sikkink LA

PROVIDER: S-EPMC2441971 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain.

Sikkink Laura A LA Ramirez-Alvarado Marina M

Biophysical chemistry 20080318 1-3

Amyloid fibrils are associated with sulfated glycosaminoglycans in the extracellular matrix. The presence of sulfated glycosaminoglycans is known to promote amyloid formation in vitro and in vivo, with the sulfate groups playing a role in this process. In order to understand the role that sulfate plays in amyloid formation, we have studied the effect of salts from the Hofmeister series on the protein structure, stability and amyloid formation of an amyloidogenic light chain protein, AL-12. We ha ...[more]

PMID: 18395318

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2008-01-26 | GSE10273 | GEO

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