Protein misfolding and aggregation

Protein Misfolding and Aggregation Are Associated with Some Neurological Diseases... 

Protein misfolding and aggregation are now known to be J/ an important feature of several human diseases. These maladies are referred to as conformational diseases, because they are believed to be caused, at least in part, by abnormal conformational changes in certain proteins. Prominent examples include Alzheimer s disease and Creutzfeld-Jacob disease. Each is discussed briefly. 

Cassland and Jonsson [13] suggested that the higher recombinant protein yield often observed at lower temperatures is caused by a decrease in protein misfolding and aggregation, as well as a reduction in proteolytic degradation. The existence of proteases... 

The underlying molecular and energetic origins for protein misfolding and aggregation (for review see refs. 38 and 39-42) leading to amyloidosis and disorders like, e.g. the transmissible spongiform encephalopathies (TSEs) and Alzheimer s disease (AD) are still an open question. 

Jaenicke, R. (1995). Folding and association versus misfolding and aggregation of proteins. Philos. Trans. R. Soc. Lond. B Biol. Sci. 348, 97-105. 

Protein Folding, Misfolding and Aggregation Classical Themes and Novel Approaches... 

These hydrophobic patches, especially in the restricted and constrained environments of the cell, may lead to misfolding and aggregate formation. Molecular chaperones minimize the off-pathway events that decrease the yield of the stable and native form of the protein, and assist the unfolded conformation to fold correctly to the native form. 

The problem of in vitro protein folding has become a major barrier to the successful use of bacterial systems for protein production. Bacterial hosts often produce inactive protein in the form of inclusion bodies. The refolding of this inactive protein results in the recovery of the native molecules as well as misfolded and aggregated proteins. Aggregate formation reduces the yield of... 

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