Atomic Force Microscopy Study of Peptides Homologous to Beta-Domain of Alpha-Lactalbumins

Title: Atomic Force Microscopy Study of Peptides Homologous to Beta-Domain of Alpha-Lactalbumins

Volume: 14 Issue: 5

Author(s): V. V. Egorov, K. V. Solovyov, N. A. Grudinina, D. V. Lebedev, V. V. Isaev-Ivanov, O. I. Kiselev and M. M. Shawlovsky

Affiliation:

Keywords: alpha-lactalbumin, fibrillogenesis, gydtqaivennesteyg, gydtqtvvnnnghtdyg, symmetry, atomic force microscopy

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 betadomain 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.

Cite this article as:

Egorov V. V., Solovyov V. K., Grudinina A. N., Lebedev V. D., Isaev-Ivanov V. V., Kiselev I. O. and Shawlovsky M. M., Atomic Force Microscopy Study of Peptides Homologous to Beta-Domain of Alpha-Lactalbumins, Protein & Peptide Letters 2007; 14 (5) . https://dx.doi.org/10.2174/092986607780782858