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The two faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity

Journal Article


Abstract


  • Molecular chaperones are a diverse group of proteins that stabilize 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, ParkinsonÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs and HuntingtonÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs 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 casein proteins, ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿS2- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein, have a propensity to assemble into amyloid fibrils under physiological conditions. The fibril-forming propensity of ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs2- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein, the possibility of its occurrence in mammary tissue, and the ability of the other casein proteins, ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs1- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein, to inhibit the aggregation of ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs2- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein and other proteins, are discussed. The results have application in the use of casein proteins in a systematic manner to stabilise other proteins at high temperature and under shear conditions, as occurs in the industrial treatment of milk and milk-based products.

Authors


  •   Thorn, David C. (external author)
  •   Ecroyd, Heath
  •   Carver, John A. (external author)

Publication Date


  • 2009

Citation


  • Thorn, D., Ecroyd, H. & Carver, J. A. (2009). The two faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity. Australian Journal of Dairy Technology, 64 (1), 34-40.

Scopus Eid


  • 2-s2.0-63749124891

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/942

Number Of Pages


  • 6

Start Page


  • 34

End Page


  • 40

Volume


  • 64

Issue


  • 1

Abstract


  • Molecular chaperones are a diverse group of proteins that stabilize 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, ParkinsonÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs and HuntingtonÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs 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 casein proteins, ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿS2- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein, have a propensity to assemble into amyloid fibrils under physiological conditions. The fibril-forming propensity of ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs2- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein, the possibility of its occurrence in mammary tissue, and the ability of the other casein proteins, ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs1- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein, to inhibit the aggregation of ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿs2- and ÃÂÃÂÃÂÃÂÃÂÃÂÃÂÿ-casein and other proteins, are discussed. The results have application in the use of casein proteins in a systematic manner to stabilise other proteins at high temperature and under shear conditions, as occurs in the industrial treatment of milk and milk-based products.

Authors


  •   Thorn, David C. (external author)
  •   Ecroyd, Heath
  •   Carver, John A. (external author)

Publication Date


  • 2009

Citation


  • Thorn, D., Ecroyd, H. & Carver, J. A. (2009). The two faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity. Australian Journal of Dairy Technology, 64 (1), 34-40.

Scopus Eid


  • 2-s2.0-63749124891

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/942

Number Of Pages


  • 6

Start Page


  • 34

End Page


  • 40

Volume


  • 64

Issue


  • 1