Open Access. Powered by Scholars. Published by Universities.®

Life Sciences Commons

Open Access. Powered by Scholars. Published by Universities.®

External Link

Social and Behavioral Sciences

2011

Chaperone

Articles 1 - 2 of 2

Full-Text Articles in Life Sciences

The Effect Of Small Molecules In Modulating The Chaperone Activity Of Alpha B-Crystallin Against Ordered And Disordered Protein Aggregation, Heath Ecroyd, John Carver Dec 2011

The Effect Of Small Molecules In Modulating The Chaperone Activity Of Alpha B-Crystallin Against Ordered And Disordered Protein Aggregation, Heath Ecroyd, John Carver

Heath Ecroyd

Protein aggregation can proceed via disordered or ordered mechanisms, with the latter being associated with amyloid fibril formation, which has been linked to a number of debilitating conditions including Alzheimer's, Parkinson's and Creutzfeldt-Jakob diseases. Small heat-shock proteins (sHsps), such as alpha B-crystallin, act as chaperones to prevent protein aggregation and are thought to play a key role in the prevention of protein-misfolding diseases. In this study, we have explored the potential for small molecules such as arginine and guanidine to affect the chaperone activity of alpha B-crystallin against disordered (amorphous) and ordered (amyloid fibril) forms of protein aggregation. The effect …


The Two Faced Nature Of Milk Casein Proteins: Amyloid Fibril Formation And Chaperone-Like Activity, David Thorn, Heath Ecroyd, John Carver Dec 2011

The Two Faced Nature Of Milk Casein Proteins: Amyloid Fibril Formation And Chaperone-Like Activity, David Thorn, Heath Ecroyd, John Carver

Heath Ecroyd

Molecular chaperones are a diverse group of proteins that stabilise partially folded target proteins to prevent their misfolding, aggregation and potential precipitation under conditions of cellular stress, e.g. elevated temperature. Protein aggregation, particularly the formation of highly ordered protein aggregates termed amyloid fibrils, is of considerable research interest because of its intimate association with a wide range of debilitating diseases, including Alzheimer's, Parkinson's and Huntington's diseases and type II diabetes. In this review, we discuss the ability of the milk casein proteins to act in a chaperone-like manner. This property is of biological importance since at least two of the …