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Опубликовано 2014-12-31 Опубликовано на SciPeople2015-01-06 00:30:50 ЖурналPrion

A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis.

Egorov VV, Lebedev DV, Shaldzhyan AA, Sirotkin AK, Gorshkov AN, Mirgorodskaya OA, Grudinina NA, Vasin AV, Shavlovsky MM. / Владимир Егоров

Prion 2014 Sep 3;8(5):369-73. doi: 10.4161/19336896.2014.983745.

Аннотация 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 GYDTQAIVENNESTEYG peptide solution components during fibrillogenesis. Possible mechanisms and roles of short peptides in protein metabolism are discussed.