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 Lettjournal_title
FEBS lettersauthors
Mikawa S,Mizuguchi C,Nishitsuji K,Baba T,Shigenaga A,Shimanouchi T,Sakashita N,Otaka A,Akaji K,Saito Hdoi
10.1002/1873-3468.12426subject
Has Abstractpub_date
2016-10-01 00:00:00pages
3492-3500issue
20eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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