Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases

Anna Villar-Piqué, Matthias Schmitz, Niccolò Candelise, Salvador Ventura, Franc Llorens, Inga Zerr

Research output: Contribution to journalReview articleResearchpeer-review

9 Citations (Scopus)


© 2018, Springer Science+Business Media, LLC, part of Springer Nature. The presence of protein deposits is a common pathological hallmark in patients suffering from neurodegenerative conditions and other proteinopathies. Deciphering the molecular basis of protein misfolding and aggregation is a crucial step towards the full comprehension of the factors that trigger the onset of these diseases and for the development of efficient therapeutical strategies. In this regard, in vitro aggregation assays for misfolded proteins offer an excellent tool to study pathological processes of protein deposition under controlled conditions, where confounders can be easily discriminated. These methods are generally cost-effective and have been proved useful in many fields, including drug discovery and clinical diagnostics. Here, we review the bases of in vitro aggregation and seeding assays, recapitulate their main applications and offer a critical evaluation of their limitations. Comprehending the molecular mechanisms behind these assays and combining them with in vivo or cell-based experiments will maximize their potential and allow the necessary improvement to overcome some of the current drawbacks.
Original languageEnglish
Pages (from-to)7588-7605
JournalMolecular Neurobiology
Issue number9
Publication statusPublished - 1 Sep 2018


  • In vitro aggregation assays
  • Neurodegeneration
  • Prion
  • Protein misfolding
  • Seeding


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