Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.
FEBS Lett
; 590(20): 3492-3500, 2016 Oct.
Article
in En
| MEDLINE
| ID: mdl-27654470
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 ß-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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptide Fragments
/
Heparin
/
Apolipoprotein A-I
/
Amyloid
Limits:
Humans
Language:
En
Journal:
FEBS Lett
Year:
2016
Document type:
Article
Affiliation country:
Japan
Country of publication:
ENGLAND
/
ESCOCIA
/
GB
/
GREAT BRITAIN
/
INGLATERRA
/
REINO UNIDO
/
SCOTLAND
/
UK
/
UNITED KINGDOM