0000000000850007
AUTHOR
Filippo Pullara
Early stages of beta2-microglobulin aggregation and the inhibiting action of alphaB-crystallin
The interest of nucleation of protein crystals and aggregates (including oligomerization) spans from basic physics theory all the way to biophysics, nanophysics, clinical sciences, biotechnologies, food technologies and polymer-solvent interactions. Understanding nucleation within a theoretical framework capable of providing quantitative predictions and control of nucleation rates, or even the very occurrence of crystallization, is a long-sought goal of remarkable relevance to each of the above fields. A large amount of work has been aimed at such goal, but success has been so far rather limited. Work at our laboratory has more recently highlighted a direct link between nucleation rates and…
Protein aggregation/crystallization and minor structural changes: universal versus specific aspects.
AbstractProtein association covers wide interests in biophysics, protein science, and biotechnologies, and it is often viewed as governed by conformation details. More recently, the existence of a universal physical principle governing aggregation/crystallization processes has been suggested by a series of experiments and shown to be linked to the universal scaling properties of concentration fluctuations occurring in the proximity of a phase transition (spinodal demixing in the specific case). Such properties have provided a quantitative basis for capturing kinetic association data on a universal master curve, ruled by the normalized distance of the state of the system from its instability…
Lysozyme crystallization rates controlled by anomalous fluctuations
Abstract Nucleation of protein aggregates and crystals is a process activated by statistical fluctuations of concentration. Nucleation rates may change by several orders of magnitude upon apparently minor changes in the multidimensional space of parameters (temperature, pH, protein concentration, salt type and concentrations, additives). We use available data on hen egg lysozyme crystal induction times in different solution conditions. We measure by static and dynamic light scattering the amplitudes and lifetimes of anomalously ample and long-lived fluctuations occurring in proximity of the liquid–liquid demixing region of the given lysozyme solutions. This allows determining the related sp…
Discussion on "Protein crystallization: universal thermodynamic vs. specific effects of PEG"
Protein crystallization: universal thermodynamic vs. specific effects of PEG
The interest of nucleation of protein crystals and aggregates (including oligomerization) spans from basic physics theory all the way to biophysics, nanophysics, clinical sciences, biotechnologies, food technologies and polymer–solvent interactions. Understanding nucleation within a theoretical framework capable of providing quantitative predictions and control of nucleation rates, or even the very occurrence of crystallization, is a long-sought goal of remarkable relevance to each of the above fields. A large amount of work has been aimed at such goal, but success has been so far rather limited. Work at our laboratory has more recently highlighted a direct link between nucleation rates and…
Absorption band at 7.6 eV induced by γ-irradiation in silica glasses
Optical absorption of defects induced by γ-irradiation in both natural and synthetic silica is experimentally investigated in the vacuum-ultraviolet (UV) range. Our results show that γ-rays, in a dose range of 1000 Mrad, induce an absorption band centered at 7.6 eV, the so-called E band, whose growth kinetics is not related to γ-activated precursors but to defects of the glassy matrix directly induced via the breaking of Si–O bonds occurring under γ-irradiation. Moreover, we observe that γ-rays do not bleach the E band present in some silica samples before irradiation, so ruling out that the associated defects can be precursors of the paramagnetic E′ centers, also induced by γ-irradiation.
Relation Between Liquid-Liquid Demixing and Crystallization Rates in Lysozyme plus NaCl Solutions
Aggregation Kinetics of Bovine Serum Albumin Studied by FTIR Spectroscopy and Light Scattering
To investigate which type of structural and conformational changes is involved in the aggregation processes of bovine serum albumin (BSA), we have performed thermal aggregation kinetics in D(2)O solutions of this protein. The tertiary conformational changes are followed by Amide II band, the secondary structural changes and the formation of beta-aggregates by the Amide I' band and, finally, the hydrodynamic radius of aggregates by dynamic light scattering. The results show, as a function of pD, that: tertiary conformational changes are more rapid as pD increases; the aggregation proceeds through formation of ordered aggregates (oligomers) at pD far from the isoelectric point of the protein;…