Protective interactions of dairy peptides with fibril structures and relevance to Alzheimer's Disease
Selected dairy caseins have been shown to have capacity for chaperone-like regulation of folding pathways of other caseins, specifically in preventing development of fibrillar aggregates of beta sheet structure. An assay based on fibril formation by reduced and carboxymethylated-kappa casein (RCM-kCn) was thus used to screen for anti-fibril activity among a selection of dairy protein hydrolysates, in order to discover peptides with possible anti-fibril, chaperone activity. From the selection of...[Show more]
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|Source:||The Australian Journal of Dairy Technology (Volume 64)|
|01_Bennett_Protective_interactions_of_2009.pdf||321.16 kB||Adobe PDF||Request a copy|
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