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1.
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9 p, 1.1 MB |
Atomistic fibrillar architectures of polar prion-inspired heptapeptides
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Peccati, Francesca (Centro de Investigación Cooperativa en Biociencias. Basque Research and Technology Alliance) ;
Díaz-Caballero, Marta (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Navarro, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Rodríguez Santiago, Luis (Universitat Autònoma de Barcelona. Departament de Química) ;
Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Sodupe Roure, Mariona (Universitat Autònoma de Barcelona. Departament de Química) ;
Universitat Autònoma de Barcelona.
Departament de Bioquímica i de Biologia Molecular ;
Universitat Autònoma de Barcelona.
Departament de Química
This article provides the computational prediction of the atomistic architectures resulting from self-assembly of the polar heptapeptide sequences NYNYNYN, SYSYSYS and GYGYGYG. Using a combination of molecular dynamics and a newly developed tool for non-covalent interaction analysis, we uncover the properties of a new class of bionanomaterials, including hydrogen-bonded polar zippers, and the relationship between peptide composition, fibril geometry and weak interaction networks. [...]
2020 -  10.1039/d0sc05638c
Chemical science, Vol. 11, Issue 48 (December 2020) , p. 13143-13151
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2.
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18 p, 1.7 MB |
MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments
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Martins, Pedro M. (Universidade do Porto. Instituto de Ciências Biomédicas Abel Salazar) ;
Navarro, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Silva, Alexandra (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Pinto, Maria F. (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Sárkány, Zsuzsa (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Figueiredo, Francisco (Universidade do Porto. Instituto de Ciências Biomédicas Abel Salazar) ;
Barbosa Pereira, Pedro José (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Bednarikova, Zuzana (Slovak Academy of Sciences. Department of Biophysics) ;
Burdukiewicz, Michal (Warsaw University of Technology. Faculty of Mathematics and Information Science) ;
Galzitskaya, Oxxana V. (Russian Academy of Sciences. Institute of Theoretical and Experimental Biophysics) ;
Gazova, Zuzana (Slovak Academy of Sciences. Department of Biophysics) ;
Gomes, Cláudio M. (Universidade de Lisboa. Departamento de Química e Bioquímica) ;
Pastore, Annalisa (Centre at King's College London. the Maurice Wohl Clinical Neuroscience Institute) ;
Serpell, Louise C. (University of Sussex. School of Life Sciences) ;
Skrabana, Rostislav (Slovak Academy of Sciences. Institute of Neuroimmunology) ;
Smirnovas, Vytautas (Vilnius University. Institute of Biotechnology) ;
Ziaunys, Mantas (Vilnius University. Institute of Biotechnology) ;
Otzen, Daniel E. (Aarhus University. Department of Molecular Biology and Genetics) ;
Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Macedo-Ribeiro, Sandra (Universidade do Porto. Instituto de Biologia Molecular e Celular and Instituto de Investigação e Inovação em Saúde) ;
Universitat Autònoma de Barcelona.
Departament de Bioquímica i de Biologia Molecular
Reports on phase separation and amyloid formation for multiple proteins and aggregation-prone peptides are recurrently used to explore the molecular mechanisms associated with several human diseases. [...]
2020 - 10.3389/fnmol.2020.582488
Frontiers in molecular neuroscience, Vol. 13 (November 2020) , art. 582488
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3.
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12 p, 2.4 MB |
Inhibition of α-synuclein aggregation and mature fibril disassembling with a minimalistic compound, ZPDm
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Peña Díaz, Samuel (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Santos Suárez, Jaime (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pallarès i Goitiz, Irantzu (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Navarro, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Conde Gimenez, María (Universidad de Zaragoza. Instituto Aragonés de Investigaciones Sanitarias) ;
García, Jesús (Institut de Recerca Biomèdica) ;
Salvatella, Xavier (Institució Catalana de Recerca i Estudis Avançats) ;
Dalfo Capella, Esther (Universitat Autònoma de Barcelona. Medicina) ;
Sancho, Javier (Universidad de Zaragoza. Instituto Aragonés de Investigaciones Sanitarias) ;
Ventura, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Universitat Autònoma de Barcelona.
Departament de Bioquímica i de Biologia Molecular
Synucleinopathies are a group of disorders characterized by the accumulation of α-Synuclein amyloid inclusions in the brain. Preventing α-Synuclein aggregation is challenging because of the disordered nature of the protein and the stochastic nature of fibrillogenesis, but, at the same time, it is a promising approach for therapeutic intervention in these pathologies. [...]
2020 - 10.3389/fbioe.2020.588947
Frontiers in Bioengineering and Biotechnology, Vol. 8 (October 2020) , art. 588947
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4.
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15 p, 4.1 MB |
Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity
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Carija, Anita (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pinheiro, Francisca (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Pujols, Jordi (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Brás, Inês C. (University Medicine Göttingen) ;
Lázaro, Diana Fernandes (University Medicine Göttingen) ;
Santambrogio, Carlo (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Grandori, Rita (University of Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze) ;
Outeiro, Tiago F. (Max Planck Institute for Experimental Medicine) ;
Navarro, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
The aggregation of α-synuclein (α-syn) into amyloid fibrils is a major pathological hallmark of Parkinson's disease (PD) and other synucleinopathies. The mechanisms underlying the structural transition of soluble and innocuous α-syn to aggregated neurotoxic forms remains largely unknown. [...]
2019 - 10.1016/j.redox.2019.101135
Redox biology, Vol. 22 (April 2019) , art. 101135
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5.
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12 p, 548.1 KB |
Mosaicism in Fanconi anemia : concise review and evaluation of published cases with focus on clinical course of blood count normalization
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Nicoletti, Eileen (Rocket Pharmaceuticals, Inc., New York) ;
Rao, Gayatri (Rocket Pharmaceuticals, Inc., New York, NY USA) ;
Bueren, Juan A. (Instituto de Investigaciones Sanitarias Fundación Jiménez Díaz) ;
Río, Paula (Instituto de Investigaciones Sanitarias Fundación Jiménez Díaz) ;
Navarro, Susana (Instituto de Investigaciones Sanitarias Fundación Jiménez Díaz) ;
Surrallés i Calonge, Jordi (Institut d'Investigació Biomèdica Sant Pau) ;
Choi, Grace (Rocket Pharmaceuticals, Inc., New York) ;
Schwartz, Jonathan D. (Rocket Pharmaceuticals, Inc., New York) ;
Universitat Autònoma de Barcelona.
Departament de Genètica i de Microbiologia
Fanconi anemia (FA) is a DNA repair disorder resulting from mutations in genes encoding for FA DNA repair complex components and is characterized by variable congenital abnormalities, bone marrow failure (BMF), and high incidences of malignancies. [...]
2020 - 10.1007/s00277-020-03954-2
Annals of Hematology, Vol. 99 (february 2020) , p. 913-924
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6.
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12 p, 5.4 MB |
The biofilm-associated surface protein Esp of Enterococcus faecalis forms amyloid-like fibers
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Taglialegna, Agustina (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ;
Matilla-Cuenca, Leticia (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ;
Dorado-Morales, Pedro (Universidad Pública de Navarra. Departamento de Salud) ;
Navarro, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Garnett, James A. (Centre for Host Microbiome Interactions. Dental institute. King's College London) ;
Lasa, Iñigo (Universidad Pública de Navarra. Departamento de Salud) ;
Valle, Jaione (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología)
Functional amyloids are considered as common building block structures of the biofilm matrix in different bacteria. In previous work, we have shown that the staphylococcal surface protein Bap, a member of the Biofilm-Associated Proteins (BAP) family, is processed and the fragments containing the N-terminal region become aggregation-prone and self-assemble into amyloid-like structures. [...]
2020 - 10.1038/s41522-020-0125-2
npj biofilms and microbiomes, Vol. 6, issue 1 (2020) , art. 15
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7.
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34 p, 4.2 MB |
Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals
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Taglialegna, Agustina (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ;
Navarro, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Garnett, James A. (Queen Mary University of London. School of Biological and Chemical Sciences) ;
Matthews, Steve (Imperial College London. Department of Life Sciences) ;
Penades, José R. (University of Glasgow. College of Medical, Veterinary and Life Sciences) ;
Lasa, Iñigo (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología) ;
Valle, Jaione (Consejo Superior de Investigaciones Científicas (Espanya). Instituto de Agrobiotecnología)
Biofilms are communities of bacteria that grow encased in an extracellular matrix that often contains proteins. The spatial organization and the molecular interactions between matrix scaffold proteins remain in most cases largely unknown. [...]
2016 - 10.1371/journal.ppat.1005711
PLoS pathogens, Vol. 12, issue 6 (June 2016) , p. e1005711
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9.
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16 p, 3.8 MB |
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
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Macedo, Bruno (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Sant'Anna, Ricardo (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Navarro, Susana (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Cordeiro, Yraima (Universidade Federal do Rio de Janeiro. Faculdade de Farmácia) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Background: An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. [...]
2015 - 10.1186/s12934-015-0361-y
Microbial cell factories, Vol. 14 (2015) , art. 174
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