Coaggregation of $κ$-casein and $β$-Lactoglobulin produces morphologically distinct amyloid fibrils. Raynes, J. K, Day, L., Crepin, P., Horrocks, M. H, & Carver, J. A Small, 13(14):1603591, Wiley, April, 2017. abstract bibtex The unfolding, misfolding, and aggregation of proteins lead to a variety of structural species. One form is the amyloid fibril, a highly aligned, stable, nanofibrillar structure composed of $β$-sheets running perpendicular to the fibril axis. $β$-Lactoglobulin ($β$-Lg) and $κ$-casein ($κ$-CN) are two milk proteins that not only individually form amyloid fibrillar aggregates, but can also coaggregate under environmental stress conditions such as elevated temperature. The aggregation between $β$-Lg and $κ$-CN is proposed to proceed via disulfide bond formation leading to amorphous aggregates, although the exact mechanism is not known. Herein, using a range of biophysical techniques, it is shown that $β$-Lg and $κ$-CN coaggregate to form morphologically distinct co-amyloid fibrillar structures, a phenomenon previously limited to protein isoforms from different species or different peptide sequences from an individual protein. A new mechanism of aggregation is proposed whereby $β$-Lg and $κ$-CN not only form disulfide-linked aggregates, but also amyloid fibrillar coaggregates. The coaggregation of two structurally unrelated proteins into cofibrils suggests that the mechanism can be a generic feature of protein aggregation as long as the prerequisites for sequence similarity are met.
@ARTICLE{Raynes2017-ik,
title = "Coaggregation of $\kappa$-casein and {$\beta$-Lactoglobulin}
produces morphologically distinct amyloid fibrils",
author = "Raynes, Jared K and Day, Li and Crepin, Pauline and Horrocks,
Mathew H and Carver, John A",
abstract = "The unfolding, misfolding, and aggregation of proteins lead to a
variety of structural species. One form is the amyloid fibril, a
highly aligned, stable, nanofibrillar structure composed of
$\beta$-sheets running perpendicular to the fibril axis.
$\beta$-Lactoglobulin ($\beta$-Lg) and $\kappa$-casein
($\kappa$-CN) are two milk proteins that not only individually
form amyloid fibrillar aggregates, but can also coaggregate
under environmental stress conditions such as elevated
temperature. The aggregation between $\beta$-Lg and $\kappa$-CN
is proposed to proceed via disulfide bond formation leading to
amorphous aggregates, although the exact mechanism is not known.
Herein, using a range of biophysical techniques, it is shown
that $\beta$-Lg and $\kappa$-CN coaggregate to form
morphologically distinct co-amyloid fibrillar structures, a
phenomenon previously limited to protein isoforms from different
species or different peptide sequences from an individual
protein. A new mechanism of aggregation is proposed whereby
$\beta$-Lg and $\kappa$-CN not only form disulfide-linked
aggregates, but also amyloid fibrillar coaggregates. The
coaggregation of two structurally unrelated proteins into
cofibrils suggests that the mechanism can be a generic feature
of protein aggregation as long as the prerequisites for sequence
similarity are met.",
journal = "Small",
publisher = "Wiley",
volume = 13,
number = 14,
pages = "1603591",
month = apr,
year = 2017,
keywords = "amyloid fibril; casein; coaggregation; molecular chaperone;
protein aggregation; $\beta$-lactoglobulin",
copyright = "http://onlinelibrary.wiley.com/termsAndConditions",
language = "en"
}
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One form is the amyloid fibril, a highly aligned, stable, nanofibrillar structure composed of $β$-sheets running perpendicular to the fibril axis. $β$-Lactoglobulin ($β$-Lg) and $κ$-casein ($κ$-CN) are two milk proteins that not only individually form amyloid fibrillar aggregates, but can also coaggregate under environmental stress conditions such as elevated temperature. The aggregation between $β$-Lg and $κ$-CN is proposed to proceed via disulfide bond formation leading to amorphous aggregates, although the exact mechanism is not known. Herein, using a range of biophysical techniques, it is shown that $β$-Lg and $κ$-CN coaggregate to form morphologically distinct co-amyloid fibrillar structures, a phenomenon previously limited to protein isoforms from different species or different peptide sequences from an individual protein. A new mechanism of aggregation is proposed whereby $β$-Lg and $κ$-CN not only form disulfide-linked aggregates, but also amyloid fibrillar coaggregates. The coaggregation of two structurally unrelated proteins into cofibrils suggests that the mechanism can be a generic feature of protein aggregation as long as the prerequisites for sequence similarity are met.","journal":"Small","publisher":"Wiley","volume":"13","number":"14","pages":"1603591","month":"April","year":"2017","keywords":"amyloid fibril; casein; coaggregation; molecular chaperone; protein aggregation; $β$-lactoglobulin","copyright":"http://onlinelibrary.wiley.com/termsAndConditions","language":"en","bibtex":"@ARTICLE{Raynes2017-ik,\n title = \"Coaggregation of $\\kappa$-casein and {$\\beta$-Lactoglobulin}\n produces morphologically distinct amyloid fibrils\",\n author = \"Raynes, Jared K and Day, Li and Crepin, Pauline and Horrocks,\n Mathew H and Carver, John A\",\n abstract = \"The unfolding, misfolding, and aggregation of proteins lead to a\n variety of structural species. One form is the amyloid fibril, a\n highly aligned, stable, nanofibrillar structure composed of\n $\\beta$-sheets running perpendicular to the fibril axis.\n $\\beta$-Lactoglobulin ($\\beta$-Lg) and $\\kappa$-casein\n ($\\kappa$-CN) are two milk proteins that not only individually\n form amyloid fibrillar aggregates, but can also coaggregate\n under environmental stress conditions such as elevated\n temperature. The aggregation between $\\beta$-Lg and $\\kappa$-CN\n is proposed to proceed via disulfide bond formation leading to\n amorphous aggregates, although the exact mechanism is not known.\n Herein, using a range of biophysical techniques, it is shown\n that $\\beta$-Lg and $\\kappa$-CN coaggregate to form\n morphologically distinct co-amyloid fibrillar structures, a\n phenomenon previously limited to protein isoforms from different\n species or different peptide sequences from an individual\n protein. A new mechanism of aggregation is proposed whereby\n $\\beta$-Lg and $\\kappa$-CN not only form disulfide-linked\n aggregates, but also amyloid fibrillar coaggregates. The\n coaggregation of two structurally unrelated proteins into\n cofibrils suggests that the mechanism can be a generic feature\n of protein aggregation as long as the prerequisites for sequence\n similarity are met.\",\n journal = \"Small\",\n publisher = \"Wiley\",\n volume = 13,\n number = 14,\n pages = \"1603591\",\n month = apr,\n year = 2017,\n keywords = \"amyloid fibril; casein; coaggregation; molecular chaperone;\n protein aggregation; $\\beta$-lactoglobulin\",\n copyright = \"http://onlinelibrary.wiley.com/termsAndConditions\",\n language = \"en\"\n}\n\n","author_short":["Raynes, J. K","Day, L.","Crepin, P.","Horrocks, M. H","Carver, J. 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