Light Scattering Study of Turbid Heat-Set Globular Protein Gels Using Cross-Correlation Dynamic Light Scattering

Nicolai, Taco; Urban, Claus; Schurtenberger, Peter

doi:10.1006/jcis.2001.7672

Cited by 38 publications

(29 citation statements)

References 23 publications

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“…The one-dimensional growth followed by a dynamic arrest phenomenon, observed in this work is reminiscent of the aggregation process in several protein solution systems [38,39,40,41]. In this class of protein solutions, a variation in the external control parameters (temperature, ionic strength, p.H.)…”

Section: Discussionmentioning

confidence: 70%

One-Dimensional Cluster Growth and Branching Gels in Colloidal Systems with Short-Range Depletion Attraction and Screened Electrostatic Repulsion

2005

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We report extensive numerical simulations of a simple model for charged colloidal particles in suspension with small nonadsorbing polymers. The chosen effective one-component interaction potential is composed of a short-range attractive part complemented by a Yukawa repulsive tail. We focus on the case where the screening length is comparable to the particle radius. Under these conditions, at low temperature, particles locally cluster into quasi one-dimensional aggregates which, via a branching mechanism, form a macroscopic percolating gel structure. We discuss gel formation and contrast it with the case of longer screening lengths, for which previous studies have shown that arrest is driven by the approach to a Yukawa glass of spherical clusters. We compare our results with recent experimental work on charged colloidal suspensions (Phys. Rev. Lett. 2005, 94, 208301).

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Section: Discussionmentioning

confidence: 70%

One-Dimensional Cluster Growth and Branching Gels in Colloidal Systems with Short-Range Depletion Attraction and Screened Electrostatic Repulsion

2005

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“…As a result, normally buried hydrophobic residues may act as a crosslinker for intermolecular beta-sheet structures and lead to formation of aggregates of different shapes, globular or amyloid like, depending on the solution conditions [16,31,32]. Continuous heating leads to association of aggregates and subsequent formation of a gel network [16][17][18]32,33].…”

Section: Discussionmentioning

confidence: 99%

“…In aggregation through another mechanism, originated from non-native contacts, alteration in conformation of proteins due to heat or physical stress may lead to the formation of irreversible aggregates [6,12,13]. Depending on the pH and ionic strength of solution and at high enough protein concentrations [14,15], by prolong heating, the aggregates associate and eventually can form a gel network [16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Effects of Protein Unfolding on Aggregation and Gelation in Lysozyme Solutions

et al. 2020

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In this work, we investigate the role of folding/unfolding equilibrium in protein aggregation and formation of a gel network. Near the neutral pH and at a low buffer ionic strength, the formation of the gel network around unfolding conditions prevents investigations of protein aggregation. In this study, by deploying the fact that in lysozyme solutions the time of folding/unfolding is much shorter than the characteristic time of gelation, we have prevented gelation by rapidly heating the solution up to the unfolding temperature (~80 °C) for a short time (~30 min.) followed by fast cooling to the room temperature. Dynamic light scattering measurements show that if the gelation is prevented, nanosized irreversible aggregates (about 10–15 nm radius) form over a time scale of 10 days. These small aggregates persist and aggregate further into larger aggregates over several weeks. If gelation is not prevented, the nanosized aggregates become the building blocks for the gel network and define its mesh length scale. These results support our previously published conclusion on the nature of mesoscopic aggregates commonly observed in solutions of lysozyme, namely that aggregates do not form from lysozyme monomers in their native folded state. Only with the emergence of a small fraction of unfolded proteins molecules will the aggregates start to appear and grow.

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“…In short, static light scattering intensity over a broad range of protein concentrations is used to describe and magnify non‐ideality of scattering behaviour at increasing solute concentrations due to PPI. Non‐ideality can be related to changes in molecule shape, packing or protein clustering . As a result, scattering intensity increases (or decreases) in a nonlinear way at elevated protein concentrations because of attractive (or repulsive) PPI.…”

Section: Methodsmentioning

confidence: 99%

Low-volume solubility assessment during high-concentration protein formulation development

Hofmann

Winzer

Weber

et al. 2016

Journal of Pharmacy and Pharmacology

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Light Scattering Study of Turbid Heat-Set Globular Protein Gels Using Cross-Correlation Dynamic Light Scattering

Cited by 38 publications

References 23 publications

One-Dimensional Cluster Growth and Branching Gels in Colloidal Systems with Short-Range Depletion Attraction and Screened Electrostatic Repulsion

One-Dimensional Cluster Growth and Branching Gels in Colloidal Systems with Short-Range Depletion Attraction and Screened Electrostatic Repulsion

Effects of Protein Unfolding on Aggregation and Gelation in Lysozyme Solutions

Low-volume solubility assessment during high-concentration protein formulation development

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