AGGRESCAN: Method, application, and perspectives for drug design

Natalia S. De Groot, Virginia Castillo, Ricardo Graña-Montes, Salvador Ventura

Research output: Contribution to journalArticleResearchpeer-review

51 Citations (Scopus)


Protein aggregation underlies the development of an increasing number of conformational human diseases of growing incidence, such as Alzheimer's and Parkinson's diseases. Furthermore, the accumulation of recombinant proteins as intracellular aggregates represents a critical obstacle for the biotechnological production of polypeptides. Also, ordered protein aggregates constitute novel and versatile nanobiomaterials. Consequently, there is an increasing interest in the development of methods able to forecast the aggregation properties of polypeptides in order to modulate their intrinsic solubility. In this context, we have developed AGGRESCAN, a simple and fast algorithm that predicts aggregation-prone segments in protein sequences, compares the aggregation properties of different proteins or protein sets and analyses the effect of mutations on protein aggregation propensities. © 2012 Springer Science+Business Media, LLC.
Original languageEnglish
Pages (from-to)199-220
JournalMethods in Molecular Biology
Publication statusPublished - 23 Jan 2012


  • Amyloid
  • Biomaterials
  • Inclusion bodies
  • Protein aggregation
  • Protein misfolding
  • Protein production


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