title: Crowded milieu prevents fibrillation of hen egg white lysozyme with retention of enzymatic activity.
abstract: Molten globule state plays a crucial role in the amyloidogenesis of several proteins. Hen egg white lysozyme (HEWL) acquires a molten globule state at alkaline pH (12.75). Our study reveals a significant inhibitory effect of high molecular weight polyethylene glycols (PEG) (PEG 20000 and PEG 35000) against alkali-salt mediated fibrillation of HEWL. Native state of HEWL is stabilized in the presence of PEGs accompanied by a decrease in the β-sheet content. Enzymatic activity of HEWL is mostly retained in the presence of polyethylene glycols. The comparable hydrodynamic radius (Rh) of PEG 20000 and native HEWL is central reason to the greater inhibitory potency of PEG 20000 against HEWL fibrillation.
authors.affiliation: Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
authors.forename: Sudeshna
authors.initials: S
authors.lastname: Ghosh
authors.affiliation: Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
authors.forename: Nitin K
authors.initials: NK
authors.lastname: Pandey
authors.affiliation: Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India. Electronic address: swagata@chem.iitkgp.ernet.in.
authors.forename: Swagata
authors.initials: S
authors.lastname: Dasgupta
mesh_terms: D000818:Animals; D052160:Benzothiazoles; D002645:Chickens; D004789:Enzyme Activation; D057446:Hydrodynamics; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000737:chemistry / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013844:Thiazoles / Q000737:chemistry / Q000378:metabolism
chemical_list: D052160:Benzothiazoles; D013844:Thiazoles; C009462:thioflavin T; D011092:Polyethylene Glycols; C421864:hen egg lysozyme; D009113:Muramidase
keywords: Enzymatic activity; Fibrillation; Hen egg white lysozyme; Hydrodynamic radius; Inhibition; PEG