Inherent Aggregation Propensity of Flanking Residues Attached to Polyglutamines: Implication to Aggregation Inhibition

Title:Inherent Aggregation Propensity of Flanking Residues Attached to Polyglutamines: Implication to Aggregation Inhibition

Volume: 20 Issue: 5

Author(s): Kalyan Sundar Ghosh

Affiliation:

Keywords: PolyQ aggregation, flanking residues, chaperone

Abstract: Expansion of polyglutamine (polyQ) sequence in some proteins leads to their aggregation, which is responsible for neurodegenerative diseases like Huntington’s disease, ataxia etc. A flanking domain is usually fused at the N-terminal to polyQ in these proteins. On linking the flanking residues to polyQ, they accelerate aggregation of the proteins, which initiates from the flanking residues. In this report the inherent propensity of the flanking residues towards aggregation in six aggregating proteins has been elucidated from their primary sequences with the help of Betascan and PASTA programs and explored unambiguously. This will provide a molecular mechanism of this process. Suppression of aggregation using chaperones like αB-crystallin by masking the exposed hydrophobic surface of flanking residues is also documented through molecular docking, which could be applied for inhibition of aggregation of this type of proteins.

Cite this article as:

Sundar Ghosh Kalyan, Inherent Aggregation Propensity of Flanking Residues Attached to Polyglutamines: Implication to Aggregation Inhibition, Protein & Peptide Letters 2013; 20 (5) . https://dx.doi.org/10.2174/0929866511320050010

DOI https://dx.doi.org/10.2174/0929866511320050010	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305