期刊
BIOPHYSICAL CHEMISTRY
卷 135, 期 1-3, 页码 25-31出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2008.02.019
关键词
amyloid; protein stability; hofineister salts; immunoglobulin light chain; light chain amyloidosis
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM071514] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM071514, R01 GM071514-03, GM 071514] Funding Source: Medline
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 50(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. (c) 2008 Elsevier B.V. All rights reserved.
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