Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.

Abstract:

:Glycosaminoglycans are known to be associated with extracellular amyloid deposits of various amyloidogenic proteins. In this study, we found that the glycosaminoglycan heparin greatly accelerates the elongation step in fibril formation by the N-terminal 1-83 fragment of human apolipoprotein A-I (apoA-I), especially in the amyloidogenic W50R variant. Using fragment peptides, we demonstrate that heparin significantly promotes β-transition and fibril formation of the highly amyloidogenic region spanning residues 44-65 and colocalizes with fibrils formed by the W50R variant. These results suggest the possible role of glycosaminoglycans in fibril formation by amyloidogenic apoA-I variants.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Mikawa S,Mizuguchi C,Nishitsuji K,Baba T,Shigenaga A,Shimanouchi T,Sakashita N,Otaka A,Akaji K,Saito H

doi

10.1002/1873-3468.12426

subject

Has Abstract

pub_date

2016-10-01 00:00:00

pages

3492-3500

issue

20

eissn

0014-5793

issn

1873-3468

journal_volume

590

pub_type

信件
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