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Issue 97, 2019
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Tryptophan–glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations

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Abstract

Glycosylation of amyloidogenic proteins enhances their solubility and reduces propensity for aggregation. We therefore, prepared tryptophan–glucosamine conjugates to modulate aggregation of tau-derived PHF6-peptide. Combined in vitro and in silico approaches indicated that these conjugates inhibited oligomerization and fibril formation of PHF6 and disrupted its preformed fibrils at very low concentration. These effects mainly arise from the glucopyranoside moiety.

Graphical abstract: Tryptophan–glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations

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Publication details

The article was received on 03 Sep 2019, accepted on 08 Nov 2019 and first published on 12 Nov 2019


Article type: Communication
DOI: 10.1039/C9CC06868F
Chem. Commun., 2019,55, 14621-14624

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    Tryptophan–glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations

    A. Paul, W. Li, G. K. Viswanathan, E. Arad, S. Mohapatra, G. Li, R. Jelinek, E. Gazit, Y. Li and D. Segal, Chem. Commun., 2019, 55, 14621
    DOI: 10.1039/C9CC06868F

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