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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Intermedios cinéticos en el conjunto amiloide.

Chen Liang1, Rong Ni, Jillian E Smith

  • 1Departments of Chemistry and Biology, Emory University , Atlanta, Georgia 30322, United States.

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|October 15, 2014
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Los conjuntos de péptidos amiloides de la enfermedad de Alzheimer se forman a través de transiciones conformacionales, no por maduración de Ostwald. Se descubrieron nuevos mecanismos para las vías de nucleación de la enfermedad de Alzheimer utilizando métodos estructurales avanzados.

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Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Estructural Biología estructural.
  • La neurociencia es la neurociencia.

Sus antecedentes:

  • Los ensamblajes amiloides están implicados en la patogénesis de la enfermedad de Alzheimer.
  • El modelo típico para el crecimiento amiloide es la maduración tipo Ostwald.

Objetivo del estudio:

  • Para investigar el mecanismo de nucleación del péptido Aβ mutante holandés en la enfermedad de Alzheimer.
  • Para dilucidar los intermediarios estructurales durante el ensamblaje amiloide.

Principales métodos:

  • Espectroscopia de infrarrojos (IR) con edición de isótopos.
  • Espectroscopia de resonancia magnética nuclear (RMN) en estado sólido.

Principales resultados:

  • Se observó una serie de transiciones conformacionales durante la nucleación, en contraste con la maduración de tipo Ostwald.
  • Se identificó una orientación inesperada de las hebras en conjuntos intermedios.
  • Caracterizó la vía de ensamblaje progresivo del núcleo amiloide.

Conclusiones:

  • La nucleación del péptido mutante holandés Aβ implica distintas transiciones conformacionales.
  • Estos hallazgos sugieren nuevos mecanismos de nucleación para la formación de amiloide en la enfermedad de Alzheimer.
  • La vía de ensamblaje progresivo proporciona nuevos conocimientos sobre la estructura del amiloide.