Найдено научных статей и публикаций: 2, для научной тематики: GYDTQAIVENNESTEYG
1.
Egorov VV, Lebedev DV, Shaldzhyan AA, Sirotkin AK, Gorshkov AN, Mirgorodskaya OA, Grudinina NA, Vasin AV, Shavlovsky MM.
- Prion , 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 demonstrat...
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.
Prion 2014 Sep 3;8(5):369-73. doi: 10.4161/19336896.2014.983745.
2.
Egorov V.V., Solovyov K. V., Grudinina N. A., Lebedev D. V., Isaev-Ivanov V. V., Kiselev O. I., Shawlovsky M. M.
- Protein Peptide Letters , 2007
Symmetrical peptide GYDTQAIVENNESTEYG (WT, Wild Type) identical to 35-51 aminoacid residues of human alpha-lactalbumin (HLA) and peptide GYDTQTVVNNNGHTDYG (ID, IDeal symmetry) homologous to beta-domain of mammalian alpha-lactalbumins can form amyloid-like fibrils in conditions required for fibrillo...
Symmetrical peptide GYDTQAIVENNESTEYG (WT, Wild Type) identical to 35-51 aminoacid residues of human alpha-lactalbumin (HLA) and peptide GYDTQTVVNNNGHTDYG (ID, IDeal symmetry) homologous to beta-domain of mammalian alpha-lactalbumins can form amyloid-like fibrils in conditions required for fibrillogenesis of HLA. The latter peptide can also form fibrils in deionized water. Fibrils formed by these peptides can cause forming of HLA amyloid-like aggregates in physiological conditions. These results provide an evidence for presence of amyloidogenic determinant in beta-domain of alpha-lactalbumin. Thus, symmetry in the primary structure may play the role in fibrillogenesis of proteins
Protein and peptide letters 14(5): 411-414, 2007
