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

Laura A. Sikkink, Marina Ramirez-Alvarado

Research output: Contribution to journalArticle

37 Citations (Scopus)

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 SO42- 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.

Original languageEnglish (US)
Pages (from-to)25-31
Number of pages7
JournalBiophysical Chemistry
Volume135
Issue number1-3
DOIs
StatePublished - Jun 2008

Fingerprint

Immunoglobulin Light Chains
Protein Stability
Amyloid
Salts
A73025
salts
proteins
Proteins
Sulfates
sulfates
Ions
augmentation
Extracellular Matrix
ions
Light
Water
matrices
water

Keywords

  • Amyloid
  • Hofmeister salts
  • Immunoglobulin light chain
  • Light Chain Amyloidosis
  • Protein stability

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Physical and Theoretical Chemistry

Cite this

Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain. / Sikkink, Laura A.; Ramirez-Alvarado, Marina.

In: Biophysical Chemistry, Vol. 135, No. 1-3, 06.2008, p. 25-31.

Research output: Contribution to journalArticle

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