Role of the C-terminal 28 residues of beta2-microglobulin in amyloid fibril formation.

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

Biochemistry

journal_title

Biochemistry

authors

Ivanova MI,Gingery M,Whitson LJ,Eisenberg D

doi

10.1021/bi0301486

subject

Has Abstract

pub_date

2003-11-25 00:00:00

pages

13536-40

issue

46

eissn

0006-2960

issn

1520-4995

journal_volume

42

pub_type

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