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Updated: Dec 17, 2025

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
Published on: February 27, 2018
The β-turn-supporting motif in the polyglutamine binding peptide QBP1 is essential for inhibiting huntingtin
Vinay Kumar Belwal1, Debika Datta1, Nitin Chaudhary1
1Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, India.
Abstract:
Aggregation of polyglutamine proteins is a hallmark of several neurodegenerative diseases. The 11-residue polyglutamine binding peptide Ac-SNWKWWPGIFD-am, known as QBP1, inhibits polyglutamine aggregation. Besides, a minimal 8-residue stretch in the QBP1 peptide (Ac-WKWWPGIF-am) is reported in the literature to retain this activity. Both peptides harbor a Pro-Gly dipeptide motif, a feature characteristic of potential β-turn regions. Here, we investigated whether the presence of this β-turn motif is necessary for the inhibition of huntingtin aggregation, a polyglutamine protein implicated in Huntington's disease. Using single amino acid substitutions to generate analogs that could support, introduce, or eliminate the β-turn, we show that the turn-supporting motif is essential for QBP1-mediated inhibition of huntingtin aggregation.
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