The crowd you're in with: Effects of different types of crowding agents on protein aggregation

What Can the Kinetics of Amyloid Fibril Formation Tell about Off-pathway Aggregation?

“…This is because the adopted equilibrium concentrations for amyloid (C a * ) and off-pathway (C off * ) aggregates are expected to differ substantially from the real thermodynamic solubilities. Not only are the solutions highly concentrated and nonideal, but also the chemical potential of the solute seems to be drastically influenced by the presence of aggregates in a process akin to volume exclusion effects (49). The asymptotic HEWL concentration of 0.75 mM estimated for long reaction times implies that aggregation assays conducted at concentrations below this limit would not produce off-pathway precipitates, let alone amyloid fibrils.…”

Biophysical insight into the anti-amyloidogenic behavior of taurine

“…In addition to protein associated with diseases other proteins such as lysozyme, serum albumins, insulin, etc. also form amyloids under suitable conditions like high temperature, low pH, in presence of surfactants, oxidation, ionic strength and crowding agents [8][9][10]. Number of evidences are available that proves that morphological and histochemical properties of disease associated or disease unrelated proteins are very similar which suggests that fibril formation is the intrinsic property of all polypeptide [11].…”

Introducing Protein Intrinsic Disorder

“…98 Osmolytes tend to stabilize function-related secondary structure of IDPs, as usually demonstrated by CD spectroscopy. 53 Crowding by Dextran and Ficoll-70 does elicit some compaction but not folding of IDPs, 42,99,100 as demonstrated on different IDPs under different conditions and using a variety of techniques. 101 It appears that the formation of local secondary structural elements of IDPs is promoted by crowding and thus preformed structural elements (PSEs) may receive even more credit than suggested by in vitro studies.…”