title: Involvement of non-polyalanine (polyA) residues in aggregation of polyA proteins: Clue for inhibition of aggregation.
abstract: Presence of polyalanine (polyA) stretches in some proteins is found to be associated with their aggregation, which causes disorders in various developmental processes. In this work, inherent propensities towards aggregation of some residues, which are not part of the polyA stretches, have been identified by using the primary sequences of seven polyA proteins with the help of Betascan, PASTA and Tango programs and explored unambiguously. This provides a basis for proposing molecular mechanism of this type of aggregation. Reported suppression of aggregation of polyA proteins by chaperones like HSP40 and HSP70 is substantiated through molecular docking. The hydrophobic residues of identified aggregating region are found to be interacting with hydrophobic surface of chaperones. This suggests a crucial clue for possible way to inhibit the aggregation of such proteins.
authors.affiliation: Department of Chemistry, National Institute of Technology Hamirpur, Himachal Pradesh 177005, India.
authors.forename: Vandna
authors.initials: V
authors.lastname: Sharma
authors.affiliation: Department of Chemistry, National Institute of Technology Hamirpur, Himachal Pradesh 177005, India. Electronic address: kalyansg5@gmail.com.
authors.forename: Kalyan Sundar
authors.initials: KS
authors.lastname: Ghosh
keywords: Docking; HSP40; HSP70; Hydrophobic interaction; PolyA aggregation