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

doi:10.1039/c9cc06868f

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

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

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.

Original language	English
Pages (from-to)	14621-14624
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	97
DOIs	https://doi.org/10.1039/c9cc06868f
State	Published - 1 Jan 2019

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Catalysis
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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title = "Tryptophan-glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations",

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.",

author = "Ashim Paul and Li, {Wen Hao} and Viswanathan, {Guru Krishna Kumar} and Elad Arad and Satabdee Mohapatra and Gao Li and Raz Jelinek and Ehud Gazit and Li, {Yan Mei} and Daniel Segal",

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T1 - Tryptophan-glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations

AU - Paul, Ashim

AU - Li, Wen Hao

AU - Viswanathan, Guru Krishna Kumar

AU - Arad, Elad

AU - Mohapatra, Satabdee

AU - Li, Gao

AU - Jelinek, Raz

AU - Gazit, Ehud

AU - Li, Yan Mei

AU - Segal, Daniel

PY - 2019/1/1

Y1 - 2019/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85076002808&partnerID=8YFLogxK

U2 - 10.1039/c9cc06868f

DO - 10.1039/c9cc06868f

M3 - Article

AN - SCOPUS:85076002808

SN - 1359-7345

VL - 55

SP - 14621

EP - 14624

JO - Chemical Communications

JF - Chemical Communications

IS - 97

ER -

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

Abstract

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