TY - JOUR
T1 - Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain
AU - Sikkink, Laura A.
AU - Ramirez-Alvarado, Marina
N1 - Funding Information:
We thank Roshini Abraham for providing us with the cDNA for AL-12, Whyte Owen for insight about the Hofmeister series, Grazia Isaya, Heather Thompson and the Ramirez-Alvarado lab for helpful discussions. This study was supported by NIH GM071514, American Heart Association SDG 063007N, and the Mayo Foundation.
PY - 2008/6
Y1 - 2008/6
N2 - 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.
AB - 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.
KW - Amyloid
KW - Hofmeister salts
KW - Immunoglobulin light chain
KW - Light Chain Amyloidosis
KW - Protein stability
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U2 - 10.1016/j.bpc.2008.02.019
DO - 10.1016/j.bpc.2008.02.019
M3 - Article
C2 - 18395318
AN - SCOPUS:43049148991
SN - 0301-4622
VL - 135
SP - 25
EP - 31
JO - Biophysical Chemistry
JF - Biophysical Chemistry
IS - 1-3
ER -