@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"
}

{"_id":"bDTkS8CA6dn2e83pK","bibbaseid":"raynes-day-crepin-horrocks-carver-coaggregationofcaseinandlactoglobulinproducesmorphologicallydistinctamyloidfibrils-2017","author_short":["Raynes, J. K","Day, L.","Crepin, P.","Horrocks, M. H","Carver, J. A"],"bibdata":{"bibtype":"article","type":"article","title":"Coaggregation of $κ$-casein and $β$-Lactoglobulin produces morphologically distinct amyloid fibrils","author":[{"propositions":[],"lastnames":["Raynes"],"firstnames":["Jared","K"],"suffixes":[]},{"propositions":[],"lastnames":["Day"],"firstnames":["Li"],"suffixes":[]},{"propositions":[],"lastnames":["Crepin"],"firstnames":["Pauline"],"suffixes":[]},{"propositions":[],"lastnames":["Horrocks"],"firstnames":["Mathew","H"],"suffixes":[]},{"propositions":[],"lastnames":["Carver"],"firstnames":["John","A"],"suffixes":[]}],"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 $β$-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. A"],"bibbaseid":"raynes-day-crepin-horrocks-carver-coaggregationofcaseinandlactoglobulinproducesmorphologicallydistinctamyloidfibrils-2017","role":"author","urls":{},"keyword":["amyloid fibril; casein; coaggregation; molecular chaperone; protein aggregation; $β$-lactoglobulin"],"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/f/SnzpCnctps9apFAde/MyRefs.bib","dataSources":["6RizfyANYFwZbeYCF","hos8GKTiSWJrJ8p57","jYJBHEqqdSqSw3E7J","DrBTLzMk52FTGMmNJ"],"keywords":["amyloid fibril; casein; coaggregation; molecular chaperone; protein aggregation; $β$-lactoglobulin"],"search_terms":["coaggregation","casein","lactoglobulin","produces","morphologically","distinct","amyloid","fibrils","raynes","day","crepin","horrocks","carver"],"title":"Coaggregation of $κ$-casein and $β$-Lactoglobulin produces morphologically distinct amyloid fibrils","year":2017}