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

Ashim Paul, Wen Hao Li, Guru Krishna Kumar Viswanathan, Elad Arad, Satabdee Mohapatra, Gao Li, Raz Jelinek, Ehud Gazit, Yan Mei Li, Daniel Segal*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)14621-14624
Number of pages4
JournalChemical Communications
Issue number97
StatePublished - 2019


FundersFunder number
National Natural Science Foundation of China
Israel Science Foundation
Tsinghua University
Tel Aviv University


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