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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
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Tryptophan-glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations.
Ashim Paul1, Wen-Hao Li, Guru KrishnaKumar Viswanathan
1School of Molecular Cell Biology & Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel. dsegal@post.tau.ac.il.
Chemical Communications (Cambridge, England)
|November 21, 2019
Summary
Tryptophan-glucosamine conjugates were synthesized to inhibit the aggregation of tau-derived PHF6-peptide. These compounds effectively reduced peptide oligomerization and fibril formation, with effects attributed to the glucopyranoside component.
Area of Science:
- Biochemistry
- Neuroscience
- Chemical Biology
Background:
- Amyloidogenic proteins, such as tau, are prone to aggregation.
- Protein glycosylation can enhance solubility and reduce aggregation propensity.
Purpose of the Study:
- To investigate the potential of tryptophan-glucosamine conjugates in modulating the aggregation of tau-derived PHF6-peptide.
- To explore the structural basis for the anti-aggregation effects.
Main Methods:
- Synthesis of tryptophan-glucosamine conjugates.
- In vitro assays to assess PHF6-peptide aggregation.
- In silico modeling to understand molecular interactions.
Main Results:
- Tryptophan-glucosamine conjugates significantly inhibited PHF6-peptide oligomerization and fibril formation.
- Preformed PHF6 fibrils were disrupted by the conjugates at low concentrations.
- The glucopyranoside moiety was identified as the primary driver of these inhibitory effects.
Conclusions:
- Tryptophan-glucosamine conjugates are effective inhibitors of tau-derived PHF6-peptide aggregation.
- Glycosylation, specifically via the glucopyranoside moiety, offers a promising strategy for developing therapeutics against amyloidogenic protein aggregation.
