Journal article
Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones α3- and β-casein
DC Thorn, S Meehan, M Sunde, A Rekas, SL Gras, CE MacPhee, CM Dobson, MR Wilson, JA Carver
Biochemistry | Published : 2005
DOI: 10.1021/bi051352r
Abstract
Caseins are a unique and diverse group of proteins present in bovine milk. While their function is presumed to be primarily nutritional, caseins have a remarkable ability to stabilize proteins, i.e., to inhibit protein aggregation and precipitation, that is comparable to molecular chaperones of the small heat-shock protein (sHsp) family. Additionally, sHsps have been shown to inhibit the formation of amyloid fibrils. This study investigated (i) the fibril-forming propensities of casein proteins and their mixture, sodium caseinate, and (ii) the ability of caseins to prevent in vitro fibril formation by κ-casein. Transmission electron microscopy (TEM) and X-ray fiber diffraction data demonstra..
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