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Published 2007-06-25 Published on SciPeople2009-04-25 09:25:16 OrganizationОМРБ ПИЯФ РАН, ГУ НИИ гриппа РАМН, ГУ НИИЭМ РАМН JournalProtein Peptide Letters

Atomic force microscopy study of peptides homologous to beta-domain of alpha-lactalbumins

Egorov V.V., Solovyov K. V., Grudinina N. A., Lebedev D. V., Isaev-Ivanov V. V., Kiselev O. I., Shawlovsky M. M. / Владимир Егоров

Protein and peptide letters 14(5): 411-414, 2007

Abstract 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