Tryptophan–glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations
| Autor: | Wen-Hao Li, Raz Jelinek, Ehud Gazit, Ashim Paul, Yan-Mei Li, Elad Arad, Guru KrishnaKumar Viswanathan, Gao Li, Daniel L. Segal, Satabdee Mohapatra |
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| Rok vydání: | 2019 |
| Předmět: |
Glycosylation
010405 organic chemistry Chemistry In silico Metals and Alloys Tryptophan macromolecular substances General Chemistry 010402 general chemistry Fibril 01 natural sciences Catalysis In vitro 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials chemistry.chemical_compound Biochemistry Glucosamine Materials Chemistry Ceramics and Composites Moiety Solubility |
| Zdroj: | Chemical Communications. 55:14621-14624 |
| ISSN: | 1364-548X 1359-7345 |
| DOI: | 10.1039/c9cc06868f |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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