The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases

Cremades, N. (Universidad de Zaragoza) ; Dobson, C.M.

Resumen: Many neurodegenerative disorders, including Alzheimer''s, Parkinson''s and the prion diseases, are characterized by a conformational conversion of normally soluble proteins or peptides into pathological species, by a process of misfolding and self-assembly that leads ultimately to the formation of amyloid fibrils. Recent studies support the idea that multiple intermediate species with a wide variety of degrees of neuronal toxicity are generated during such processes. The development of a high level of knowledge of the nature and structure of the pathogenic amyloid species would significantly enhance efforts to underline the molecular origins of these disorders and also to develop both accurate diagnoses and effective therapeutic interventions for these types of conditions. In this review, we discuss recent biophysical and structural information concerning different types of amyloid aggregates and the way in which such information can guide rational therapeutic approaches designed to target specific pathogenic events that occur during the development of these highly debilitating and increasingly common diseases.

Idioma: Inglés

DOI: 10.1016/j.nbd.2017.07.009

Año: 2018

Publicado en: NEUROBIOLOGY OF DISEASE 109 (2018), 178-190
ISSN: 0969-9961

Factor impacto JCR: 5.16 (2018)

Categ. JCR: NEUROSCIENCES rank: 47 / 266 = 0.177 (2018) - Q1 - T1

Factor impacto SCIMAGO: 2.665 - Neurology (Q1)

Tipo y forma: Revisión (Versión definitiva)

Área (Departamento): Área Bioquímica y Biolog.Mole. (Dpto. Bioq.Biolog.Mol. Celular)