title: Characterization of the nucleation process of lysozyme at physiological pH: primary but not sole process.
abstract: We report on a kinetic study of the heat-induced aggregation process of lysozyme at physiological pH. The time evolution of the aggregation extent and the conformational changes of the protein were followed by dynamic light scattering (DLS) and FTIR spectroscopy, respectively, whereas the morphology of the aggregates was observed by Atomic Force Microscopy (AFM). The conformational changes of the secondary and tertiary structures were simultaneous and distinct in time with respect to the formation of aggregates. Oligomer formation occurred through at least two different aggregation processes: a nucleation process and a homogeneous non-nucleative diffusion-controlled process. FTIR measurements showed that supramolecular aggregation proceeded without the formation of β-aggregated structures and AFM images revealed the presence of oligomers and amorphous aggregates; no fibrillar structures were observed.
authors.affiliation: Dipartimento di Fisica e Chimica, Università di Palermo, Palermo, Italy. giovanna.navarra@unipa.it
authors.forename: Giovanna
authors.initials: G
authors.lastname: Navarra
authors.forename: Filippo
authors.initials: F
authors.lastname: Troia
authors.forename: Valeria
authors.initials: V
authors.lastname: Militello
authors.forename: Maurizio
authors.initials: M
authors.lastname: Leone
mesh_terms: D000818:Animals; D002645:Chickens; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D008027:Light; D018625:Microscopy, Atomic Force; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
chemical_list: D009113:Muramidase