Your browser doesn't support javascript.
loading
Localized conformational changes trigger the pH-induced fibrillogenesis of an amyloidogenic λ light chain protein.
Velázquez-López, Isabel; Valdés-García, Gilberto; Romero Romero, Sergio; Maya Martínez, Roberto; Leal-Cervantes, Ana I; Costas, Miguel; Sánchez-López, Rosana; Amero, Carlos; Pastor, Nina; Fernández Velasco, D Alejandro.
Afiliación
  • Velázquez-López I; Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México.
  • Valdés-García G; Centro de Investigación en Dinámica Celular, IICBA, Universidad Autónoma del Estado de Morelos, México.
  • Romero Romero S; Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México.
  • Maya Martínez R; Centro de Investigaciones Químicas, IICBA, Universidad Autónoma del Estado de Morelos, México.
  • Leal-Cervantes AI; Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México.
  • Costas M; Laboratorio de Biofisicoquímica, Departamento de Fisicoquímica, Facultad de Química, Universidad Nacional Autónoma de México, México.
  • Sánchez-López R; Instituto de Biotecnología, Universidad Nacional Autónoma de México, México.
  • Amero C; Centro de Investigaciones Químicas, IICBA, Universidad Autónoma del Estado de Morelos, México.
  • Pastor N; Centro de Investigación en Dinámica Celular, IICBA, Universidad Autónoma del Estado de Morelos, México. Electronic address: nina@uaem.mx.
  • Fernández Velasco DA; Laboratorio de Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México. Electronic address: fdaniel@unam.mx.
Biochim Biophys Acta Gen Subj ; 1862(7): 1656-1666, 2018 Jul.
Article en En | MEDLINE | ID: mdl-29669263
Solvent conditions modulate the expression of the amyloidogenic potential of proteins. In this work the effect of pH on the fibrillogenic behavior and the conformational properties of 6aJL2, a model protein of the highly amyloidogenic variable light chain λ6a gene segment, was examined. Ordered aggregates showing the ultrastructural and spectroscopic properties observed in amyloid fibrils were formed in the 2.0-8.0 pH range. At pH <3.0 a drastic decrease in lag time and an increase in fibril formation rate were found. In the 4.0-8.0 pH range there was no spectroscopic evidence for significant conformational changes in the native state. Likewise, heat capacity measurements showed no evidence for residual structure in the unfolded state. However, at pH <3.0 stability is severely decreased and the protein suffers conformational changes as detected by circular dichroism, tryptophan and ANS fluorescence, as well as by NMR spectroscopy. Molecular dynamics simulations indicate that acid-induced conformational changes involve the exposure of the loop connecting strands E and F. These results are compatible with pH-induced changes in the NMR spectra. Overall, the results indicate that the mechanism involved in the acid-induced increase in the fibrillogenic potential of 6aJL2 is profoundly different to that observed in κ light chains, and is promoted by localized conformational changes in a region of the protein that was previously not known to be involved in acid-induced light chain fibril formation. The identification of this region opens the potential for the design of specific inhibitors.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cadenas lambda de Inmunoglobulina / Agregado de Proteínas / Amiloide Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochim Biophys Acta Gen Subj Año: 2018 Tipo del documento: Article Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cadenas lambda de Inmunoglobulina / Agregado de Proteínas / Amiloide Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochim Biophys Acta Gen Subj Año: 2018 Tipo del documento: Article Pais de publicación: Países Bajos