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- W2004987777 abstract "Casein is the best characterized milk protein and constitutes over 70-80% of total bovine milk protein. In milk, casein exists as large micelle-like particles that comprise four unrelated proteins (αs1-, αs2-, β-, and κ-casein) and calcium phosphate. Although αs1-, αs2-, β-, and κ-casein present important structural differences, all of them adopt extremely open and flexible conformations, enough to be defined intrinsically disordered proteins (IDPs). Caseins are able to inhibiting protein aggregation and amyloid fibrils formation and this chaperon-like activity could be largely due to their structural disorder. In the present study we discuss the meaning of “disorder” in the case of three caseins α, β and k that have similar unordered structure and different sequence. We correlate the different type and disorder degree to the capability of preventing protein aggregation and amyloid formation. The physical-chemical parameters of α, β and k caseins were compared to those of intrinsically unfolded and ideally globular proteins. Moreover, caseins sequences were analyzed by several publicly available disorder-oriented predictors two metaservers, MeDor and metaPRDOS, and by a neural network algorithm (PONDR). We observed that α, β and k caseins have different degree and type of disorder, depending on the parameters under analysis and criteria used by the different predictors. These data were correlated to experimental results (ThT fluorescence, CD) on the caseins effect on 1-40 β-amyloid peptide fibrillogenesis. Experiments showed that k-casein forms ordered aggregates and that it is able to significantly increase lag-time and reduce fibril amount in Aβ amyloid formation. Our results contribute to clear the role of intrinsically disordered proteins and their mechanism of action by functional order/disorder transitions, and offer insight in the field of prevention and therapy in Alzheimer diseases, and, in general, of amyloid pathologies." @default.
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- W2004987777 date "2013-01-01" @default.
- W2004987777 modified "2023-09-30" @default.
- W2004987777 title "Intrinsic Disorder and Chaperon-Like Activity of Different Caseins" @default.
- W2004987777 doi "https://doi.org/10.1016/j.bpj.2012.11.2169" @default.
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