title: Effect of osmolytes on the fibrillation of HypF-N.
abstract: We have studied the effect of a series of stabilizing and destabilizing osmolytes on the fibrillation pattern of a model amyloidogenic protein, HypF-N. Under mildly denaturing conditions, HypF-N forms cross β-sheet structures, characteristic of amyloid fibrils. In the presence of all stabilizing osmolytes except proline, fibrillation of HypF-N is inhibited. Notably, fibrillation kinetics is retarded at subdenaturing concentrations of chaotropes. In case of proline, fibrillation of HypF-N is accelerated. Thus, the changes during exposure of a protein to denaturing conditions in the presence of osmolyes cannot be extrapolated from their role as anti-fibrillation agents.
authors.affiliation: Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar, Punjab 160 062, India.
authors.forename: Rupen D
authors.initials: RD
authors.lastname: Bhavsar
authors.forename: Shivcharan
authors.initials: S
authors.lastname: Prasad
authors.forename: Ipsita
authors.initials: I
authors.lastname: Roy
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000187:drug effects; D019878:Carboxyl and Carbamoyl Transferases / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry*; D007700:Kinetics; D011108:Polymers / Q000494:pharmacology; D011392:Proline / Q000494:pharmacology*; D011489:Protein Denaturation; D017510:Protein Folding / Q000187:drug effects*; D017433:Protein Structure, Secondary / Q000187:drug effects
chemical_list: D000682:Amyloid; D029968:Escherichia coli Proteins; D011108:Polymers; C024617:polyol; D011392:Proline; D019878:Carboxyl and Carbamoyl Transferases; C504838:hypF protein, E coli
keywords: Fibrillation; HypF-N; Osmolytes; Polyols; Proline