Web of Science: 23 cites, Scopus: 26 cites, Google Scholar: cites,
Computational prediction of protein aggregation : advances in proteomics, conformation-specific algorithms and biotechnological applications
Santos, Jaime (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Pujols, Jordi (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")

Data: 2020
Resum: Protein aggregation is a widespread phenomenon that stems from the establishment of non-native intermolecular contacts resulting in protein precipitation. Despite its deleterious impact on fitness, protein aggregation is a generic property of polypeptide chains, indissociable from protein structure and function. Protein aggregation is behind the onset of neurodegenerative disorders and one of the serious obstacles in the production of protein-based therapeutics. The development of computational tools opened a new avenue to rationalize this phenomenon, enabling prediction of the aggregation propensity of individual proteins as well as proteome-wide analysis. These studies spotted aggregation as a major force driving protein evolution. Actual algorithms work on both protein sequences and structures, some of them accounting also for conformational fluctuations around the native state and the protein microenvironment. This toolbox allows to delineate conformation-specific routines to assist in the identification of aggregation-prone regions and to guide the optimization of more soluble and stable biotherapeutics. Here we review how the advent of predictive tools has change the way we think and address protein aggregation.
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades. Creative Commons
Llengua: Anglès
Document: Article ; recerca ; Versió publicada
Matèria: A3D, AGGRESCAN3D ; APRs, Aggregation-prone regions ; DI, Developability index ; IAPP, Islet amyloid polypeptide ; IDPs, Intrinsically disordered proteins ; Mabs, Monoclonal antibodies ; SAP, Spatial aggregation propensity ; STAP, STructural Aggregation-Prone region ; Protein aggregation ; Bioinformatics ; Amyloid ; Protein structure ; Proteomics ; Evolution ; Protein production
Publicat a: Computational and Structural Biotechnology Journal, Vol. 18 (June 2020) , p. 1403-1413, ISSN 2001-0370

Adreça alternativa: https://europepmc.org/articles/PMC7322485
DOI: 10.1016/j.csbj.2020.05.026
PMID: 32637039


11 p, 1.4 MB

El registre apareix a les col·leccions:
Documents de recerca > Documents dels grups de recerca de la UAB > Centres i grups de recerca (producció científica) > Ciències de la salut i biociències > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Articles de recerca
Articles > Articles publicats

 Registre creat el 2020-07-13, darrera modificació el 2022-03-05



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