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

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

Journal Name: Protein & Peptide Letters

Volume 14 , Issue 5 , 2007

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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.

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

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Article Details

Year: 2007
Page: [471 - 474]
Pages: 4
DOI: 10.2174/092986607780782858
Price: $65

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