Journal
BIOPHYSICAL CHEMISTRY
Volume 177, Issue -, Pages 24-33Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2013.03.004
Keywords
Protein aggregation; Nucleation process; Dynamic light scattering; FTIR spectroscopy; AFM
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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 beta-aggregated structures and AFM images revealed the presence of oligomers and amorphous aggregates; no fibrillar structures were observed. (C) 2013 Elsevier B.V. All rights reserved.
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