6533b873fe1ef96bd12d58d5
RESEARCH PRODUCT
Characterization of the nucleation process of lysozyme at physiological pH: Primary but not sole process
Giovanna NavarraFilippo TroiaValeria MilitelloMaurizio Leonesubject
LightNucleation proceBiophysicsSupramolecular chemistryNucleationmacromolecular substancesProtein aggregationMicroscopy Atomic ForceBiochemistryOligomerProtein Structure Secondarychemistry.chemical_compoundDynamic light scatteringSpectroscopy Fourier Transform InfraredAnimalsScattering RadiationFourier transform infrared spectroscopyCircular DichroismOrganic ChemistryTemperaturetechnology industry and agricultureHydrogen-Ion ConcentrationProtein Structure TertiaryAmorphous solidFTIR spectroscopyCrystallographychemistryChemical engineeringDynamic light scatteringMuramidaseAFMProtein aggregationLysozymeChickensdescription
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. © 2013 Elsevier B.V.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2013-07-01 | Biophysical Chemistry |