The secondary structure of human amyloid deposits as determined by circular dichroism spectroscopy.
The deposition of amyloid fibrils has been associated with a diversity of pathologies including plasma cell dyscrasias, chronic inflammatory diseases, and several types of neurological diseases including Alzheimer's disease. Using circular dichroism spectroscopy, the secondary structure of a human amyloid protein deposit from a patient with plasma cell (light chain)-associated amyloidosis (amyloidosis AL) has been determined. The protein contains 52% beta structure, which is consistent with these depositions arising from the aberrant catabolism of immunoglobulin light chains, which are rich in beta sheets. The protein was also found to contain 20% alpha-helix, suggesting that partial refolding may occur during amyloidogenesis.
Department of Chemistry, Rensselaer Polytechnic Institute, Troy, New York 12180.
M
M
Cascio
P A
PA
Glazer
B A
BA
Wallace
D000596:Amino Acids / Q000032:analysis; D000682:Amyloid / Q000648:ultrastructure*; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006860:Hydrogen Bonding; D008970:Molecular Weight; D011487:Protein Conformation
D000596:Amino Acids; D000682:Amyloid