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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