title: Structural model of amyloid fibrils for amyloidogenic peptide from Bgl2p-glucantransferase of S. cerevisiae cell wall and its modifying analog. New morphology of amyloid fibrils.
abstract: We performed a comparative study of the process of amyloid formation by short homologous peptides with a substitution of aspartate for glutamate in position 2 - VDSWNVLVAG (AspNB) and VESWNVLVAG (GluNB) - with unblocked termini. Peptide AspNB (residues 166-175) corresponded to the predicted amyloidogenic region of the protein glucantransferase Bgl2 from the Saccharomyces cerevisiae cell wall. The process of amyloid formation was monitored by fluorescence spectroscopy (FS), electron microscopy (EM), tandem mass spectrometry (TMS), and X-ray diffraction (XD) methods. The experimental study at pH3.0 revealed formation of amyloid fibrils with similar morphology for both peptides. Moreover, we found that the morphology of fibrils made of untreated ammonia peptide is not mentioned in the literature. This morphology resembles snakes lying side by side in the form of a wave without intertwining. Irrespective of the way of the peptide preparation, the rate of fibril formation is higher for AspNB than for GluNB. However, preliminary treatment with ammonia highly affected fibril morphology especially for AspNB. Such treatment allowed us to obtain a lag period during the process of amyloid formation. It showed that the process was nucleation-dependent. With or without treatment, amyloid fibrils consisted of ring-like oligomers with the diameter of about 6nm packed either directly ring-to-ring or ring-on-ring with a slight shift. We also proposed the molecular structure of amyloid fibrils for two studied peptides.
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia.
authors: Olga M
authors: OM
authors: Selivanova
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia; Institute of Mathematical Problems of Biology RAS, Keldysh Institute of Applied Mathematics of Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
authors: Anna V
authors: AV
authors: Glyakina
authors: Branch of Federal State Budgetary Research Institution, "M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences", Nauka Pr. 4, 142290 Pushchino, Moscow Region, Russia.
authors: Elena Yu
authors: EY
authors: Gorbunova
authors: Branch of Federal State Budgetary Research Institution, "M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences", Nauka Pr. 4, 142290 Pushchino, Moscow Region, Russia.
authors: Leila G
authors: LG
authors: Mustaeva
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia.
authors: Mariya Yu
authors: MY
authors: Suvorina
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia.
authors: Elizaveta I
authors: EI
authors: Grigorashvili
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia.
authors: Alexey D
authors: AD
authors: Nikulin
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia.
authors: Nikita V
authors: NV
authors: Dovidchenko
authors: Department of Molecular Biology, Faculty of Biology, Moscow State University, Moscow, Russia.
authors: Valentina V
authors: VV
authors: Rekstina
authors: Department of Molecular Biology, Faculty of Biology, Moscow State University, Moscow, Russia.
authors: Tatyana S
authors: TS
authors: Kalebina
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia; State Research Center for Applied Microbiology & Biotechnology, Obolensk, Serpukhov District, Moscow Region 142279, Russia.
authors: Alexey K
authors: AK
authors: Surin
authors: Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia. Electronic address: ogalzit@vega.protres.ru.
authors: Oxana V
authors: OV
authors: Galzitskaya
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000641:Ammonia / Q000737:chemistry; D000682:Amyloid / Q000737:chemistry / Q000648:ultrastructure*; D058227:Amyloidogenic Proteins / Q000737:chemistry / Q000648:ultrastructure*; D001224:Aspartic Acid / Q000737:chemistry*; D002473:Cell Wall / Q000737:chemistry; D018360:Crystallography, X-Ray; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000737:chemistry*; D018698:Glutamic Acid / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D060327:Solid-Phase Synthesis Techniques
chemical_list: D000682:Amyloid; D058227:Amyloidogenic Proteins; D010446:Peptide Fragments; D029701:Saccharomyces cerevisiae Proteins; D001224:Aspartic Acid; D018698:Glutamic Acid; D000641:Ammonia; C080389:BGL2 protein, S cerevisiae; D004693:Glucan Endo-1,3-beta-D-Glucosidase
keywords: Amyloid fibrils; Amyloidogenic regions; Electron microscopy; Molecular structure; Oligomer; Tandem mass spectrometry; X-ray analysis