Egorov V.V.,RAS Petersburg Nuclear Physics Institute |
Lebedev D.V.,RAS Petersburg Nuclear Physics Institute |
Shaldzhyan A.A.,FSBI Research Institute of Influenza |
Sirotkin A.K.,FSBI Research Institute of Influenza |
And 5 more authors.
Prion | Year: 2014
The fibrillogenesis of a peptide corresponding to residues 35-51 of human α-lactalbumin (1GYDTQAIVENNESTEYG17) can be dramatically enhanced by the addition of a tetrapeptide TDYG homologous to its C-terminus (TEYG). Generation of spontaneous hydrolytic products similar to this peptide was demonstrated by mass-spectrometry analysis of GYDTQAIVE NNESTEYG peptide solution components during fibrillogenesis. Possible mechanisms and roles of short peptides in protein metabolism are discussed. © 2014 Taylor & Francis Group, LLC.