title: Amyloid fibril formation and other aggregate species formed by human serum albumin association.
abstract: Under in vitro solution conditions where the native state is destabilized, many proteins present an abnormal structure and metabolism associated with a strong tendency to self-aggregation into a polymeric amyloid fibril structure, suggesting that this ability is a generic feature of the polypeptide chains. Such structures play a key role in different pathogenesis of neurodegenerative diseases such as Alzheimer, Parkinson, or Creutzfeldt-Jakob. Here, we report the formation of amyloid fibrils in the plasma protein human serum albumin under different in vitro conditions monitored using a combination of spectrophotometric and microscopic techniques. Amyloid fibril formation, therefore, is also allowed in a protein with a high degree of structural complexity. We also infer from experimental data the existence of other protein aggregated species than fibrils, some of which seem to be formed by a structural rearrangement of the proper fibrils.
authors.forename: Pablo
authors.initials: P
authors.lastname: Taboada
authors.forename: Silvia
authors.initials: S
authors.lastname: Barbosa
authors.forename: Emilio
authors.initials: E
authors.lastname: Castro
authors.forename: Víctor
authors.initials: V
authors.lastname: Mosquera
mesh_terms: D000682:Amyloid / Q000138:chemical synthesis / Q000737:chemistry*; D019281:Dimerization; D006801:Humans; D008853:Microscopy; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*; D013057:Spectrum Analysis
chemical_list: D000682:Amyloid; D012709:Serum Albumin