title: AGGRESCAN: method, application, and perspectives for drug design.
abstract: 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.
authors.affiliation: Department de Bioquímica i Biologia Molecular and Institut de Biotecnologia i de Biomedicina, Universitat Autónoma de Barcelona, Barcelona, Spain.
authors.forename: Natalia S
authors.initials: NS
authors.lastname: de Groot
authors.forename: Virginia
authors.initials: V
authors.lastname: Castillo
authors.forename: Ricardo
authors.initials: R
authors.lastname: Graña-Montes
authors.forename: Salvador
authors.initials: S
authors.lastname: Ventura
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D015195:Drug Design; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D010455:Peptides / Q000737:chemistry; D011228:Prealbumin / Q000737:chemistry; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D016229:Amyloid beta-Peptides; D010455:Peptides; D011228:Prealbumin; D011506:Proteins