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Formation

Heath Ecroyd

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Dissociation From The Oligomeric State Is The Rate-Limiting Step In Fibril Formation By Kappa-Casein, Heath Ecroyd, Tomas Koudelka, David Thorn, Danielle Williams, Glyn Devlin, Peter Hoffmann, John Carver Dec 2011

Dissociation From The Oligomeric State Is The Rate-Limiting Step In Fibril Formation By Kappa-Casein, Heath Ecroyd, Tomas Koudelka, David Thorn, Danielle Williams, Glyn Devlin, Peter Hoffmann, John Carver

Heath Ecroyd

Amyloid fibrils are aggregated and precipitated forms of protein in which the protein exists in highly ordered, long, unbranching threadlike formations that are stable and resistant to degradation by proteases. Fibril formation is an ordered process that typically involves the unfolding of a protein to partially folded states that subsequently interact and aggregate through a nucleation-dependent mechanism. Here we report on studies investigating the molecular basis of the inherent propensity of the milk protein, kappa-casein, to form amyloid fibrils. Using reduced and carboxymethylated kappa-casein ( RCM kappa-CN), we show that fibril formation is accompanied by a characteristic increase in thioflavin …


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 …