Abstract：
:Beta2microglobulin (beta2m) is the major protein component of the fibrillar amyloid deposits isolated from patients diagnosed with dialysis-related amyloidosis (DRA). While investigating the molecular mechanism of amyloid fibril formation by beta2m, we found that the beta2m C-terminal peptide of 28 residues (cbeta2m) itself forms amyloid fibrils. When viewed by electron microscopy, cbeta2m aggregates appear as elongated unbranched fibers, the morphology typical for amyloids. Cbeta2m fibers stain with Congo red and show apple-green birefringence in polarized light, characteristic of amyloids. The observation that the beta2m C-terminal fragment readily forms amyloid fibrils implies that beta2m amyloid fibril formation proceeds via interactions of amyloid forming segments, which become exposed when the beta2m subunit is partially unfolded.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Ivanova MI,Gingery M,Whitson LJ,Eisenberg Ddoi
10.1021/bi0301486subject
Has Abstractpub_date
2003-11-25 00:00:00pages
13536-40issue
46eissn
0006-2960issn
1520-4995journal_volume
42pub_type
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