Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide

نویسندگان

  • Emilie CERF
  • Rabia SARROUKH
  • Shiori TAMAMIZU-KATO
  • Leonid BREYDO
  • Sylvie DERCLAYE
  • Yves F. DUFRÊNE
  • Vasanthy NARAYANASWAMI
  • Erik GOORMAGHTIGH
  • Jean-Marie RUYSSCHAERT
  • Vincent RAUSSENS
چکیده

*Center for Structural Biology and Bioinformatics, Laboratory for Structure and Function of Biological Membranes, Faculté des Sciences, Université Libre de Bruxelles, CP 206/2, Blvd. du Triomphe, B-1050 Brussels, Belgium, †Center for the Prevention of Obesity, Cardiovascular Disease and Diabetes, Children’s Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, U.S.A., ‡Department of Molecular Biology and Biochemistry, University of California at Irvine, 3438 McGaugh Hall, Irvine, CA 92697, U.S.A., §Unité de Chimie des Interfaces, Université Catholique de Louvain, Croix du Sud 2/18, B-1348 Louvain-la-Neuve, Belgium, and ‖Department of Chemistry and Biochemistry, California State University, Long Beach, 1250 Bellflower Boulevard, Long Beach, CA 90840, U.S.A.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Polyglutamine Fibrils: New Insights into Antiparallel β-Sheet Conformational Preference and Side Chain Structure.

Understanding the structure of polyglutamine (polyQ) amyloid-like fibril aggregates is crucial to gaining insights into the etiology of at least ten neurodegenerative disorders, including Huntington's disease. Here, we determine the structure of D2Q10K2 (Q10) fibrils using ultraviolet resonance Raman (UVRR) spectroscopy and molecular dynamics (MD). Using UVRR, we determine the fibril peptide ba...

متن کامل

Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure.

Parkinson's disease is an age-related movement disorder characterized by the presence in the mid-brain of amyloid deposits of the 140-amino-acid protein AS (α-synuclein). AS fibrillation follows a nucleation polymerization pathway involving diverse transient prefibrillar species varying in size and morphology. Similar to other neurodegenerative diseases, cytotoxicity is currently attributed to ...

متن کامل

Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics.

Protein amyloid oligomers have been strongly linked to amyloid diseases and can be intermediates to amyloid fibers. β-Sheets have been identified in amyloid oligomers. However, because of their transient and highly polymorphic properties, the details of their self-association remain elusive. Here we explore oligomer structure using a model system: macrocyclic peptides. Key amyloidogenic sequenc...

متن کامل

β-Hairpin-Mediated Formation of Structurally Distinct Multimers of Neurotoxic Prion Peptides

Protein misfolding disorders are associated with conformational changes in specific proteins, leading to the formation of potentially neurotoxic amyloid fibrils. During pathogenesis of prion disease, the prion protein misfolds into β-sheet rich, protease-resistant isoforms. A key, hydrophobic domain within the prion protein, comprising residues 109-122, recapitulates many properties of the full...

متن کامل

β-Amyloid Fibril Structures, In Vitro and In Vivo

Since 1998, a great deal of progress has been made towards determining and understanding the molecular structures of amyloid fibrils, including fibrils formed by the β-amyloid peptide that is associated with Alzheimer’s disease. Much of this progress has resulted from solid state nuclear magnetic resonance (NMR) measurements, which provide experimental constraints on molecular conformations and...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2009