Ordered self-assembly of the collagenous domain of adiponectin with noncovalent interactions via glycosylated lysine residues

FEBS Letters
Ayako TakuwaTadayasu Ohkubo

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.

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Citations

Feb 18, 2016·Current Genetics·David CánovasJoseph Strauss
Jan 28, 2017·Current Opinion in Biotechnology·Kevin Strauss, Jean Chmielewski
Jun 24, 2017·Organic & Biomolecular Chemistry·Katherine R LutterothMargaret A Brimble
Jun 4, 2019·Chembiochem : a European Journal of Chemical Biology·Mathieu LalandeJean-Christophe Poully
Aug 18, 2021·Biochemical and Biophysical Research Communications·Yusi ZhangBoquan Jin

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