Modifying interprotein interactions for controlling heat-induced protein gelation

Competing Effects of Temperature and Polymer Concentration on Evolution of Re-entrant Interactions in the Nanoparticle-Block Copolymer System

“…The initial rise in the temperature ( T ≤ 55 °C) leads to the slight shifting of the ACFs toward shorter delay times. Such an initial shift in the ACF can be attributed to the increase in particle diffusion, largely due to rise in temperature . In fact, the analysis of the ACF (taking temperature into account) shows a slight increase in the effective hydrodynamic size (inset of Figure ), mostly due to the adsorption of the block copolymer on nanoparticles.…”

Evolution of the structure and interaction in the surfactant-dependent heat-induced gelation of protein

“…2,16,[20][21][22] Temperature is a critical parameter for influencing protein-surfactant interactions as it is known to affect protein conformation and drives morphological transitions in surfactants. [23][24][25][26][27][28][29] When subjected to high temperatures, proteins undergo unfolding. This gives rise to the exposure of hydrophobic segments, driving protein gelation through hydrophobic attraction.…”

“…This gives rise to the exposure of hydrophobic segments, driving protein gelation through hydrophobic attraction. [23][24][25][26][27] While the impact of temperature on the morphology of ionic surfactants is relatively limited, it can cause counter-ion dissociation, thereby altering electrostatic interactions. [28][29][30][31] In this way, temperature has the ability to modify both primary interactions dictating the formation of protein-surfactant complexes.…”

“…It is therefore interesting to probe the effect of temperature variation in a larger range on the evolution of structure and interactions in protein-surfactant dispersions, and the possibility of gel formation in the system. 19,23,32,33 In the present manuscript, we utilize the surfactant-dependent interplay of interactions to guide the temperature-driven gel formation in dispersions of bovine serum albumin (BSA) protein with the cationic surfactant, dodecyl trimethyl ammonium bromide (DTAB). BSA is a globular protein that is often studied as a model protein due to its high availability, low cost, and well characterization, as well as stable properties.…”

“…Our earlier work with BSA and sodium dodecyl sulfate (SDS) has shown that the surfactants can modify the temperature-dependent gelation of the protein. 23 However, results were limited to only one surfactant concentration and under weaker interaction due to the similar charge nature of the BSA protein and SDS surfactant. Herein, we examine the cumulative effects of temperature and surfactant concentration, covering the entire range of the binding curve from the specific binding region to cooperative binding and saturation region.…”