In:
FEBS Letters, Wiley, Vol. 590, No. 2 ( 2016-01), p. 195-201
Abstract:
Adiponectin, an anti‐atherogenic and insulin‐sensitizing adipokine, forms multiple isoforms including a trimer, a hexamer and heavier oligomers (mainly octadecamer) that determine their biological activities. We designed 89‐residue peptides containing modifications found in the collagenous domain of native adiponectin. Circular dichroism and analytical ultracentrifugation measurements showed that the peptide bearing glucosyl‐galactosyl‐hydroxylysine residues forms a stable collagen‐like triple helical structure and spontaneously assembled into an octadecamer. An assembly model mediated by noncovalent interactions via glycosylated lysine residues for the octadecamer was constructed. Our findings clarified an essential role of glycosyl modifications to coordinate the ordered self‐assembly of adiponectin.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/1873-3468.12034
Language:
English
Publisher:
Wiley
Publication Date:
2016
detail.hit.zdb_id:
1460391-3
SSG:
12
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