Atomic force microscopy study of peptides homologous to beta-domain of alpha-lactalbumins.
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.
Egorov
V V
VV
Institute for Experimental Medicine RAMS, 12, Akad. Pavlova St., Saint Petersburg, Russia. olivejra@yahoo.com
Solovyov
K V
KV
Grudinina
N A
NA
Lebedev
D V
DV
Isaev-Ivanov
V V
VV
Kiselev
O I
OI
Shawlovsky
M M
MM
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
D000682:Amyloid; D007768:Lactalbumin