title: Atomic force microscopy study of peptides homologous to beta-domain of alpha-lactalbumins.
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.
authors.affiliation: Institute for Experimental Medicine RAMS, 12, Akad. Pavlova St., Saint Petersburg, Russia. olivejra@yahoo.com
authors.forename: V V
authors.initials: VV
authors.lastname: Egorov
authors.forename: K V
authors.initials: KV
authors.lastname: Solovyov
authors.forename: N A
authors.initials: NA
authors.lastname: Grudinina
authors.forename: D V
authors.initials: DV
authors.lastname: Lebedev
authors.forename: V V
authors.initials: VV
authors.lastname: Isaev-Ivanov
authors.forename: O I
authors.initials: OI
authors.lastname: Kiselev
authors.forename: M M
authors.initials: MM
authors.lastname: Shawlovsky
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000096:biosynthesis; D006801:Humans; D007768:Lactalbumin / Q000737:chemistry* / Q000235:genetics; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D017385:Sequence Homology
chemical_list: D000682:Amyloid; D007768:Lactalbumin