Plegament de Proteines i Malalties Conformacionals

(Unitat: Proteòmica Aplicada i Enginyeria de Proteïnes)

Coordinador: Prof. Salvador Ventura  ICREA Academia AwardeeIcrea

Tel.  93 586 89 56  - Tel. Laboratori : 93 586 89 54 / Fax: 93 581 20 11

Proteins are involved in virtually every biological process. To function, these chains must fold into the unique three-dimensional structure that is characteristic for each protein. In addition, proteins almost never act in an isolated manner; they interact with other proteins in order to perform essential roles in many important cellular processes. Protein malfunction is often related to disease and thousands disease-related proteins have been identified to date. In many cases, these disorders are the outcome of a failure in their folding process and/or in their binding to one or more protein partners. 

Protein Folding

Folding of Disulfide-Rich Proteins 
We exploit the particular chemistry of disulfide bonds to characterize the folding of disulfide-rich proteins with results that illustrate a high diversity of folding mechanisms. Also, by combining kinetic studies with the structural determination of folding intermediates, we have provided new molecular clues in oxidative folding and clarified some of the major rules that govern it. 

Folding of Cell Signalling Domains
Intracellular signalling networks controls cellular behaviour, and are assembled through the interactions of proteins with one another, and with other molecules. Typically, protein interaction domains are independently folding modules that can be expressed in isolation from their host proteins while retaining their intrinsic ability to bind their physiological partners. After establishing the SH3 domain as a consistent model for the study of protein folding and binding, we plan to expand our activity to other cell signalling domains. Understanding how they fold and bind is of paramount importance since many human disorders result from breakdowns in protein binding and signal transduction.

Protein Misfolding and Aggregation

We are interested in disease-related misfolding and amyloid fibril assembly.

In vitro Models 
We have shown that amyloid formation depends on specific short amino acid stretches, opening a door for the prediction of therapeutically relevant regions in amyloid proteins. These regions are usually protected inside the protein globular structure, suggesting a selection against aggregation during evolution. Using this information, we have developed AGGRESCAN, a software for the prediction of protein aggregation propensity ( Integrating computational and experimental approaches we are studying the relationship between the sequence and the structural properties of the aggregated and toxic states of several amyloid proteins, including prions, IAPP and Aß peptide. 

In vivo Models
We have established bacteria as a simple cellular model to study in vivo protein aggregation, and demonstrated the formation in prokaryotes of oligomers and amyloid structures through selective interactions. This suggest evolutionary conserved strategies to avoid the harmful effects of protein aggregation by sequestering sticky folding intermediates into stable aggregated structures in both eukaryotes and bacteria. We are now using proteomic and genomic approaches to explore the sequential and structural determinants of amyloid formation inside eukaryotic cells using yeast as a model. 

Protein-Protein Interactions

Even though most of the relevant interactions in the cell are weak and in many cases transient, there are only few methods able to detect them in vivo. Using protein engineering we have shown that bimolecular fluorescence complementation can be implemented for the detection and high-throughput screening of weak protein binders and inhibitors of such interactions. Specifically, using this approach we have been able to correlate the antimicrobial activity of natural and designed peptides with their ability to inhibit bacterial chaperones in vivo. This opens an avenue for the design and assay of new and specific antibiotics.




Cap de Grup:

Ventura Zamora, Salvador




 Folding of Disulfide Proteins

 Protein Reviews Vol. 14 

 Editor(s): Chang, Rowen J. Y.; Ventura, Salvador (2011)

 ISBN 978-1-4419-7272-9.

 Springer. Berlin, Heidelberg & New York.    



Peer reviewed international publications


167. Fernandez, M.R. Batlle, C. Gil-Garcia, M. and Ventura, S.    
Amyloid cores in prion domains: key regulators for prion conformational conversion
Prion (in press) (2017)

166Pujols, J. Peña, S. Conde-Gimenez, M. Pinheiro, F. Navarro, S. Sancho, J. and Ventura, S.  
High-throughput screening methodology to identify alpha-synuclein aggregation inhibitors
Int J Mol Sci.  (in press) (2017)

165Piovesan, D....Ventura, S.... et al. (multiple authors)  
DisProt 7.0: a major update of the database of disordered proteins
Nucleic Acids Research 45(D1):D219-D227 (2017)


164. Lazaro, D.F. Castro-Dias, M. Carija, A. Navarro, S. Silva-Madaleno, C. Tenreiro, S. Ventura, S. and Outeiro, T.F.  
The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation
Acta Neuropathologica Communications (in press) (2016)

163Marinelli, P., Pallares, I. Navarro, S. and Ventura, S. 
Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure
Scientific Reports (in press) (2016)

162. Sant'Anna, R. Fernandez, M.R. Batlle, C. Navarro, S. de Groot, N.S.  Serpell, L. and Ventura, S. 
Characterization of Amyloid Cores in Prion Domains
Scientific Reports (in press) (2016)

161. Villar-Piqué, A. da Fonseca, T.L., Sant’Anna, R. Szegöa, E.M. Fonseca-Ornelase, L. Pinhoa, R. Carija, A. Gerhardta, E. Masaracchiaa, C. Abad-Gonzalez, E. Rossettig, G.Carlonig,P. Fernández, C.O. Foguel, D. Milosevick, I. Zweckstetter, M. Ventura, S. and Outeiro, T.F.  
Environmental and genetic factors support the dissociation between alpha-synuclein aggregation and toxicity
Proc. Natl. Acad. Sci. U S A (in press) (2016)

160. Pallares, I and Ventura, S. 
Understanding and predicting protein misfolding and aggregation: Insights from proteomics
Proteomics (in press) (2016)

159. Ventura, S. 
Editorial: Protein solubility and aggregation in bacteria
Frontiers in Microbiology (in press) (2016)

158.  López, L. C. Varea, O. Navarro, S. Carrodeguas, J.A., de Groot, N.S. Ventura, S. and Sancho, J.
Benzbromarone, Quercetin and Folic Acid Inhibit Amylin Aggregation
Int J Mol Sci.  (in press) (2016)

157. Taglialegna, A. Navarro, S. Ventura, S. Garnett, J.A. Matthews, S. Penades, J.R. Lasa, I and Valle, J. 
Staphylococcal Bap proteins build amyloid scaffold biofilm matrices in response to environmental signals
PLoS Pathogens (in press) (2016)

156. Sant'Anna, R. Gallego, P. Robinson, R.L. Pereira-Henriques, A. Ferreira, N. Pinheiro, F. Esperante, S. Pallares, I. Huertas, O. Almeida, M.R. Reixach, N. Insa, R. Velazquez-Campoy, A. Reverter, D. Reig, N. and Ventura, S. 
Repositioning Tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity
Nature Communications 7:10787 (2016)

155Pallares, I and Ventura, S.
Una nueva molécula para el tratamiento de la amiloidosis familiar
Genetica Medica News (Spanish) 3(49):10-12 (2016)

154Carija, A. Navarro, S. and Ventura, S.
Data on correlation between Abeta42 structural aggregation propensity and toxicity in bacteria
Data in Brief (in press) (2016)

153Macedo, B. Cordeiro Y. and Ventura, S. 
Mammalian Prion Amyloid Formation in Bacteria
Prion (in press) (2016)

152.  Pulido, P. Llamas, E. Llorente, B. Ventura, S. Wright, L.P. and Rodriguez-Concepcion, M.
Specific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in Arabidopsis
PLoS Genetics 12(1):e1005824 (2016)

151. Sant'anna, R. Navarro, S. Ventura, S. Paraoan, L. and Foguel, D.
Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and Macular Degeneration
FEBS Letters 590(5):644-54 (2016)

150Pallares, I. Iglesias, V.  and Ventura, S. 
The Rho Termination Factor of Clostridium botulinum contains a Prion-Like Domain with a highly Amyloidogenic Core
Frontiers in Microbiology 6:1516 (2016)

149Ventura, S. 
Curing bacterial infections with protein aggregates
Molecular Microbiology 99(5):827-30 (2016)

148Navarro, S.  Carija, A, Muñoz-Torrero and Ventura, S. 
A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems
Eur J Med Chem. (15)30326-3 (2016)

147Graña-Montes, R., Pujols-Pujol, J. Gomez-Picanyol, C. and Ventura, S.
Prediction of Protein Aggregation and Amyloid Formation
From Protein Structure to Function with Bioinformatics, Edited by D. J. Rigden, (Springer-London, in press) (2016)

146Klionsky, D.J...Ventura, S.... et al. (multiple authors)
Guidelines for the Use and Interpretation of Assays for Monitoring Autophagy (3rd edition)
Autophagy 12(1):1-222 (2016)

145Villar-Pique, A. Espargaro, A. Ventura, S. and Sabate, R.
In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time
Biotechnology Journal 11(1):172-7 (2016)


144Macedo, B. Sant'anna, R. Navarro, S.  Cordeiro Y. and Ventura, S. 
Mammalian Prion Protein (PrP) Forms Conformationally Different Amyloid Intracellular Aggregates in Bacteria
Microbial Cell Factories, 14(1):174 (2015)

143Iglesias, V.  de Groot, n.S. and Ventura, S. 
Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role
Frontiers in Microbiology, 6:1123 (2015)

142Navarro, S. Marinelli, P. Diaz-Caballero,M. and Ventura, S. 
The Prion-like RNA-processing protein HNRPDL forms Inherently Toxic Amyloid-like Amyloid-like Inclusion Bodies in Bacteria
Microbial Cell Factories, 14:102 (2015)

141Martinez-Olivan, J. Fraga, H. Arias-Moreno, X. Ventura, S. and Sancho, J
Intradomain confinement of disulfides in the folding of two consecutive modules of the LDL receptor
PLoS ONE 10(7):e0132141 (2015)

140Roque, A. Sortino, R. Ventura, S. Ponte, I and Suau, P.
Histone H1 favors folding and parallel fibrillar aggregation of the 1-42 amyloid-β peptide
Langmuir, 31(24):6782-90 (2015)

139. Sabate, R. Rousseau, F. Schymkowitz, J. Batlle, C. and Ventura, S.
Amyloids or Prions? That is the question.
Prion, 9(3):200-6 (2015)

138. Zambrano, R. Jamroz, M. Szczasiuk, A. Pujols, J. Kmiecik, S. and VenturaS.
AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures
Nucleic Acids Research 43(W1):W306-13 (2015) 

137. Zambrano, R. Conchillo-Sole, O. Iglesias, V., Illa, R. Rousseau, F. Schymkowitz, J. Sabate, R. Daura, X. and Ventura, S.
PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores
Nucleic Acids Research, 43(W1):W331-7 (2015) 

136. Fraga, H and Ventura, S.
Influence of cytoplasmatic folding on mitochondrial import
Current Medicinal Chemisty, 22(19):2349-59 (2015) 

135. de Groot, NS. Gomes, RA. Villar-Pique, A. Babu, MM. Coelho, AV. and Ventura, S.
Proteome response at the edge of protein aggregation
Open Biology, 5(2):140221 (2015) 

134. Sabate, R. Rousseau, F. Schymkowitz, J. and Ventura, S. 
What makes a protein sequence a prion?
PLoS Computational Biology 10.1371/journal.pcbi.1004013 (2015) 

133. Graña-Montes, R. and Ventura, S.
Protein Aggregation and its Prediction
Multifaceted Roles of Crystallography in Modern Drug Discovery. NATO Science for Peace and Security Serie A: Chemistry and Biology. Springer pp 115-127 (2015)

132- Villar-Pique A. Navarro, S. and Ventura S. 
Characterization of amyloid-like properties in bacterial intracellular aggregates
Methods in Molecular Biology. Humana Press. Springer. New York. 1258:99-122 (2015)

131- Ventura, S. 
Protein Misfolding Diseases
Future Science OA 1(2), FSO38 (2015)

130-  Moles, E., Valle-Delgado, J.J., Urbán, P., G. Azcárate, I., Bautista, J.M., Ventura, S. and Fernàndez-Busquets, X.
Possible roles of amyloids in malaria pathophysiology
Future Science OA 1(2), FSO43 (2015)

129-  Navarro, S., Diaz-Caballero, M. Illa, R. and Ventura S. 
Aggregation propensity of neuronal receptors: Potential implications in neurodegenerative disorders
Future Science OA 1(2), FSO39 (2015)

128-  Fernandez-Busquets, X., de Groot, N.S. and Ventura, S.
Recent structural and computational insights into conformational diseases: A review
Frontiers in Medicinal Chemistry 7, 134-182 (49), Bentham Science Publishers Ltd  (2015)


127. Garcia-Pardo, J., Graña-Montes, R. Fernandez-Mendez, M. Ruyra R., Roher, N., Aviles, F.X. Lorenzo, J. and Ventura, S.
Amyloid Formation by Human Carboxypeptidase D Transthyretin-like Domain Under Native Conditions.
Journal of Biological Chemistry 289(49):33783-96 (2014)

126-  Navarro, S. and Ventura, S. 
ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli
Biotechnology Journal 9(10):1259-66 (2014)

125-  Sant’Anna R, Braga C, Varejão N, Pimenta KM, Graña-Montes R, Alves A, Cortines J, Cordeiro Y, Ventura S and Foguel D
The importance of a gatekeeper residue on the aggregation of transthyretin: implications to transthyretin-related amyloidoses
Journal of Biological Chemistry 298(41):28324-37 (2014)

124- Chutna O, Gonçalves S, Villar-Piqué A, Guerreiro P, Marijanovic Z, Mendes T, Ramalho J, Emmanouilidou E, Ventura S, Klucken, JBarral DC., Giorgini F,  Vekrellis K and Outeiro TF.
The small GTPase Rab11 co-localizes with alpha-synuclein in intracellular inclusions and modulates its aggregation and secretion
Human Molecular Genetics 23(25):6732-45 (2014)

123-  M. Polajnar, K. Škerget, T. Zavašnik-Bergant, M. Vizovišek, R. Vidmar, M. Fonović, N. Kopitar-Jerala, U. Petrovič, S. Navarro, S. Ventura and E. Žerovnik
Human stefin B role in cell’s response to misfolded proteins and autophagy
PLoS ONE 9(7):e102500 (2014)

122-  Fraga, H. Graña-Montes, R. Illa, R. Covaleda, G. and Ventura, S.
Association between Foldability and Aggregation Propensity in Small Disulfide-Rich Proteins
Antioxidants and Redox Signaling 21(3):368-83 (2014)

121- Fraga, H. Bech-Serra, J.J., Canals, F. Ortega, G., Millet, O. and Ventura, S.
The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19
Journal of Biological Chemistry 289(14):9852-64 (2014)

120- Graña-Montes, R., Marinelli, P., Reverter, D. and Ventura, S.
N-terminal Protein Tails act as Aggregation Protective Entropic Bristles: The SUMO case.
Biomacromolecules 15(4):1194-203 (2014)

119- Angarica, V.E., Angulo, A., Giner, A., Losilla, G., Ventura, S., and Sancho, J. 
PrionScan: an online database of predicted prion domains in complete proteomes.
BMC Genomics 15:102 (2014)

118- Navarro, S., Villar-Pique, A. and Ventura S. 
Selection against toxic aggregation-prone protein sequences in bacteria
BBA - Molecular Cell Research 1843(5):866-74 (2014)

117- Espargaró A., Villar-Pique A., Ventura S. and Sabate R.,
Screening for amyloid aggregation: In-silico, in-vitro and in-vivo detection
Current Protein and Peptide Science 15(5):477-89 (2014)

116- S Pouplana, A Espargaró, C Galdeano, E Viayna, I Sola, S Ventura, D Muñoz-Torrero and R Sabate 
Thioflavin-S Staining of Bacterial Inclusion Bodies for the Fast, Simple, and Inexpensive Screening of Amyloid Aggregation Inhibitors
Current Medicinal Chemistry 21(9):1152-9 (2014)

115- Villar-Pique A. and Ventura S. 
Inclusion bodies in the study of amyloid aggregation.
Protein aggregation in bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells. 93-116 (2014) Wiley series on Protein and Peptide Science ISBN: 978-1-118-44852-6.


114- Ferreira P., Sant’Anna, R., Varejão N., Lima, C., Caldeira C.M., Rumjanek F.D. Ventura S., Cruz M.W. and Foguel D.
Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy
PLoS ONE 8(12):e82484 (2013)

113- Marinelli P., Castillo V.  and Ventura S. 
Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain.
Int J Mol Sci.  14(9):17830-44 (2013)

112- Villar-Pique A. and Ventura S. 
Protein aggregation propensity is a crucial determinant of intracellular inclusions formation and quality control degradation
BBA - Molecular Cell Research 1833(12):2714-24 (2013)

111- Angarica, V.E., Ventura, S. and Sancho, J. 
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.
BMC Genomics 14:316 (2013)

110- Sabate R., Rodríguez-Santiago L., Sodupe M., Saupe S.J. and Ventura S.
Thioflavin-T Excimers Formation upon interaction with Amyloid Fibers.
Chemical Communications 49(51):5745-7 (2013)

109- Sant'Anna R. Braga C. Polikarpov I.  Ventura S. Lima L.M. and Foguel D.
Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis
Int J Mol Sci. 14, 5284-5311 (2013)

108- Castillo V. Chiti F. and Ventura S.
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain
PLoS ONE 8(3):e58297 (2013)

107- Fraga H. and Ventura S.
Oxidative Folding in the Mitochondrial Intermembrane Space in Human Health and Disease
Int J Mol Sci. 14, 2916-27 (2013)

106- Fraga H., Papaleo E., Vega S., Velazquez-Campoy, A. and Ventura S.
Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone
BBA - General Subjects 1830, 2139-49 (2013)

105-  Graña-Montes R. and Ventura S.
About Targets and Causes in Protein Folding.
Journal of Biomolecular Structure & Dynamics 31(9):970-2 (2013)

104- Sabate R. and Ventura S.
Cross-β-sheet supersecondary structure in amyloid folds: Techniques for detection and characterization.
Methods in Molecular Biology. Humana Press. Springer. New York. 932, 237-57. (2013)


103- Villar-Pique A. and Ventura S.
Modeling amyloids in bacteria
Microbial Cell Factories 11, 166 (2012)

102- Graña-Montes R., Sant'anna de Oliveira R. and Ventura S.
Protein aggregation profile of the human kinome
Frontiers in Physiology  3, 438 (2012)

101- López L.C., Dos-Reis S., Espargaró A., Carrodeguas J.A., Maddelein, M.A.,Ventura S. and Sancho J.
Discovery of novel inhibitors of amyloid β-peptide 1-42 aggregation
Journal of Medicinal Chemistry 55, 9521-30 (2012)

100- Lapidus D., Duka V.,  Czaplewski C., Liwo A.,  Ventura S. and Liepina I. 
Multiple β-sheet molecular dynamics of amyloid formation from two Abl-SH3 domain peptides.
Biopolymers. 98, 557-66 (2012)

99- Espargaró A., Sabate R. and Ventura S.
Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation
Molecular BioSystems. 8, 2839-44 (2012)

98- de Groot N.S., Torrent, M., Villar-Pique A., Lang, B. Ventura S. Gsponer J. and Babu M.M.
Evolutionary selection for protein aggregation
Biochemical Society Transactions. 40, 1032-37 (2012)

97- Villar-Pique A., Espargaró A., Sabate R., de Groot N.S. and Ventura S.
Yeast Prions Form Infectious Amyloid Inclusion Bodies in Bacteria
Microbial Cell Factories. 11, 89 (2012)

96- Invernizzi G., Papaleo E., Sabate R. and Ventura S.
Protein aggregation: mechanisms and functional consequences
The International Journal of Biochemistry & Cell Biology. 44, 1541-54 (2012)

95- Sabaté, R., Espargaro, A., Graña-Montes, R., Reverter, D. and Ventura, S.
The native structure protects SUMO proteins from aggregation into amyloid fibrils
Biomacromolecules 13,1916-26 (2012)

94- Villar-Pique A., Espargaró A., Sabate R., de Groot N.S. and Ventura S.
Using Bacterial Inclusion Bodies to Screen for Amyloid Aggregation Inhibitors
Microbial Cell Factories.11, 55 (2012)

93- Sabaté R., Espargaró A., Barbosa-Barros L., Ventura  S. and Estelrich J.
Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide.
Biochimie 94,1730-8 (2012)

92- Fraga H. and Ventura S.
Protein oxidative folding in the intermembrane mitochondrial space: More than protein trafficking.
Current Protein and Peptide Science. 13, 224-31 (2012)

91- Villar-Pique A. and Ventura S.
Protein aggregation acts as strong constraint during evolution.
Evolutionary Biology-New insights. Springer. Heidelberg, 103-120 (2012)

90- Sabate R.; Villar-Pique A.; Espargaro, A. and Ventura S.
Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions.
Biomacromolecules 13(2):474-83 (2012)

89- Villar-Pique A.; de Groot NS.; Sabate R.; Acebrón SP.; Celaya G.; Fernàndez-Busquets X.; Muga A. and Ventura S.
The effect of amyloidogenic peptides on bacterial aging  correlates with their intrinsic aggregation propensity.
Journal of Molecular Biology 421, 270-81(2012)

88- Graña-Montes R, de Groot NS, Castillo V, Sancho J, Velazquez-Campoy A, and Ventura S.
Contribution of disulfide bonds to stability, folding and amyloid fibril formation: The PI3-SH3 domain case.
Antioxidants and Redox Signaling 16, 1-15 (2012)

87- Valle-Delgado JJ, Liepina I, Lapidus D, Sabaté R, Ventura S,Samitier J, Fernàndez-Busquets X.
Self-assembly of human amylin-derived peptides studied by atomic forcemicroscopy and single molecule force spectroscopy
Soft Matter 8, 1234‐1242 (2012)

86- Ventura S.
Amyloid formation in bacteria.
Encyclopedia of Biophysics. Springer. New York. ISBN 978-3-642-16711-9 (2012)

85- de Groot N.S., Castillo V. Graña-Montes R. and Ventura S.
AGGRESCAN: Method, Application and Perspectives for Drug Design.
Methods in Molecular Biology. Humana Press. Springer. New York. 819, 199-220 (2012)


84- Ventura S.
Bimolecular Fluorescence Complementation: Illuminating cellular protein interactions
Current Molecular Medicine 11, 582‐98 (2011)

83- Morell M., de Groot N.S., Vendrell J., Aviles F.X. and Ventura S.
Linking amyloid protein aggregation and yeast survival.
Molecular BioSystems 7, 1121-8 (2011)

82- Dasari M., Espargaro A., Sabate R., Lopez Del Amo .J.M., Fink U., Grelle G., Bieschke J., Ventura S. and Reif B.
Bacterial Inclusion Bodies of the Alzheimer Disease beta-Amyloid Peptides can be employed to study Native like Aggregation Intermediate States.
ChemBioChem 12, 407-23 (2011)

81- Arolas, JL. & Ventura S.
Protease inhibitors as models for the study of oxidative folding.
Antioxidants and Redox Signaling 14, 97-112 (2011)

80- Ventura, S.
Does Stoichiometry Drive Protein Folding?
Journal of Biomolecular Structure & Dynamics 28, 655-6 (2011)

79- Castillo V., Graña-Montes R., Sabate R. and Ventura S.
Prediction of the Aggregation Propensity of Proteins from the Primary Sequence: Aggregation Properties of Proteomes.
Biotechnology Journal 6, 674-85 (2011)

78- Castillo V., Graña-Montes R. and Ventura S.
The aggregation properties of Escherichia Coli Proteins are associated with their cellular abundance.
Biotechnology Journal 6, 752-60 (2011)

77- Georgescauld, F., Sabaté, R., Espargaró, A., Ventura, S., Chaignepain, S., Lacombe, M.L., and Lascu, I.
Aggregation of the neuroblastoma-associated mutant (S120G) of the human nucleoside diphosphate kinase-A/NM23-H1 into amyloid fibrils
Naunyn-Schmiedeberg's Archives of Pharmacology 384, 373-81 (2011)

76- Chang, J.Y. & Ventura, S. Oxidative Folding
Folding of Disulfide Proteins. Protein Reviews, Vol. 14. Springer. Berlin, Heidelberg & New York.  (2011)

75-Lapidus, D., Ventura, S., Czaplewski, C. Liwo, A. and Liepina, I.
Molecular dynamics of amylin amyloid single beta-sheet.
Material Science and Applied Chemistry 23, 49-55 (2011)

74- García-Fruitós, E., Sabaté, R., de Groot, N.S., Villaverde, A. and Ventura, S.
Biological role of bacterial inclusion bodies: a model for amyloid aggregation 
FEBS Journal 278(14):2419-27.


73- de Groot N.S., & Ventura S.
Protein Aggregation Profile of the Bacterial Cytosol.
PLoS ONE 5(2):e9383 (2010)

72- Sabate, R., de Groot N.S., & Ventura S.
Protein Folding and Aggregation in Bacteria
Cellular and Molecular Life Sciences 67, 2695-715 (2010)

71- Valle-Delgado, J.J.; Alfonso-Prieto, M. S.; de Groot; N. Ventura, S.; Samitier, S.; Rovira, C.; Fernàndez-Busquets, X.
Modulation of Aβ42 fibrillogenesis by glycosaminoglycan structure
FASEB Journal 24, 4250-61 (2010)

70- Castillo V., Espargaró,A., Gordo, V. Vendrell, J. and Ventura, S.
Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria.
PROTEOMICS 10, 4172-85 (2010)

69- Sabate R.; Espargaro A.; de Groot N.S.;Valle-Delgado J.J.; Fernandez-Busquets X. and Ventura S.
The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Reading Backwards IAPP Amyloid Fibrils.
Journal of Molecular Biology 404, 337-52 (2010)

68- Villar-Piqué A., Sabaté R., Lopera, O., Gibert, J., Torne J.M., Santos, M. and Ventura, S.
Amyloid-like Protein Inclusions in Tobacco Transgenic Plants
PLoS ONE 5(10):e13625 (2010)

67- Castillo, V., Ventura S & Sabate, R.
Dye – liposome interactions: Dye localization in neutral lipid bilayers
International Review of Biophysical Chemistry 1(1), 7-13 (2010)


66- Sabate R, Espargaró A, Saupe SJ, & Ventura S.
Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion
Microbial Cell Factories 8(1):56 (2009)

65- Pantoja-Uceda D, Arolas JL, Aviles FX, Santoro J, Ventura S, & Sommerhoff CP
Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor
Journal of Biological Chemistry 284, 35612-20 (2009)

64- Castillo V, & Ventura S.
Amyloidogenic Regions and Interaction Surfaces Overlap in Globular Proteins Related to Conformational Diseases
PLoS Computational Biology 5(8):e1000476 (2009)

63- de Groot N, Sabate R & Ventura S.
Amyloids in bacterial inclusion bodies
Trends in Biochemical Sciences 34, 408-16 (2009)

62- Arolas JL, Castillo V, Bromsoms S, Aviles FX, & Ventura S
Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function
Journal of Molecular Biology 392, 529-46 (2009)

61- Liepina I, Ventura S, Czaplewski C & Liwo A.
Dynamics study on single and multiple beta-sheets
Advances in Experimental Medicine and Biology 611, 293-4 (2009)

60- Morell M, Ventura S & Avilés FX.
Protein complementation assays: Approaches for the in vivo analysis of protein interactions.
FEBS Letters 583, 1684-91 (2009)

59- Morell M, Avilés FX & Ventura S.
Detecting and interfering protein interactions: Towards the control of biochemical pathways
Current Medicinal Chemistry 16, 362-379 (2009)

58- Rodríguez-Rodríguez C, de Groot NS, Rimola A, Alvarez-Larena A, Lloveras V, Vidal-Gancedo J, Ventura S, Vendrell J, Sodupe M & González-Duarte P.
Design, selection and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer’s disease
Journal of the American Chemical Society 131, 1436-51 (2009)

57- Sabaté R, Castillo V, Espargaró A, Saupe SJ, & Ventura S.
Energy barriers for HET-s prion forming domain amyloid formation
FEBS Journal 276, 5053-64. (2009)


56- Espargaro A, Sabate R & Ventura S.
Kinetic and thermodynamic stability of bacterial intracellular aggregates.
FEBS Letters 582, 3669-73 (2008)

55- Arolas, J.L., Bronsoms, S., Aviles, F. X.,Ventura, S. and Sommerhoff, C.P.
Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates.
Antioxidants and Redox Signaling  10, 77-86 (2008)

54- Ventura, S.
Oxidative Protein Folding: From the Test Tube to in vivo insights.
Antioxidants and Redox Signaling 10, 51-54 (2008)

53- Morell, M.; Espargaro, A.; Aviles, F.X., & Ventura, S.
Study and selection of in vivo protein interactions by coupling Bimolecular Fluorescence Complementation and Flow Cytometry (BiFC-FC)
Nature Protocols 3, 22-33 (2008)

52- Fernandez-Busquets, X., Fernandez, D., de Groot, N.S. and Ventura, S.
Recent structural and computational insights into conformational diseases
Current Medicinal Chemistry 15, 1336-49 (2008)

51- Espargaro, A. Castillo, V. de Groot, N.S. & Ventura, S.
The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: The SH3 case
Journal of Molecular Biology 378, 1116-31 (2008)

50- Arias-Moreno, X.; Arolas, J.L.; Aviles, F.X.; Sancho, J.; and Ventura, S.
Scrambled isomers as key intermediates in the oxidative folding of ligand-binding module five of the LDL receptor
Journal of Biological Chemistry 283, 13627-37 (2008)

49- S. de Groot, N., Espargaro, A. Morell, M. and Ventura, S.
Studies on bacterial inclusion bodies
Future Microbiology 3, 423-35 (2008)

48- Morell M, Espargaró A, Avilés FX & Ventura S.
BIFC: a new tool for studying weak protein interactions in vivo.
Bioforum Europe 11, 31-33 (2008)

47- Morell, M., Bravo, R., Espargaro, A., Sisquella, X., Aviles, F.X., Fernandez-Busquets, X. and Ventura, S.
Inclusion Bodies: specificity in their aggregation process and amyloid-like structure
Biochim Biophys Acta. Molecular Cell Research 1783, 1815-25 (2008)

46- Morell, M., Czihal, P., Hoffmann, R., Otvos, L., Avilés, F.X. and Ventura, S.
Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation (BIFC): the DnaK case.
Proteomics 8, 3433-42 (2008)

45- Pallarès I, Fernández D, Comellas-Bigler M, Fernández-Recio J, Ventura S, Avilés FX, Bode W, Vendrell J.
Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid).
Acta Crystallogr D Biol Crystallogr. 64, 784-91 (2008)

44- Bravo R, Arimon M, Valle-Delgado JJ, García R, Durany N, Castel S, Cruz M, Ventura S, Fernàndez-Busquets X.
Sulfated polysaccharides promote the assembly of amyloid beta 1-42 peptide into stable fibrils of reduced cytotoxicity
Journal of Biological Chemistry 83, 32471-83 (2008)

43- Arolas JL, Pantoja-Uceda D, Ventura S, Blanco FJ, Aviles FX.
The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways
Journal of Biological Chemistry 283, 27110-2 (2008)


42- Pallares I, Berenguer C, Aviles FX, Vendrell J and Ventura S.
Self-assembly of human latexin into amyloid-like oligomers.
BMC Structural Biology 7:75 (2007)

41- Morell, M.; Espargaro, A.; Aviles, F.X., & Ventura, S.
Detection of Transient Protein-Protein Interactions by Bimolecular Fluorescence Complementation: The Abl-SH3 case
Proteomics 7, 1023-36 (2007)

40- S. de Groot,N.; Parella, T.;Aviles, F.X., Vendrell, J. & Ventura, S.
Ile-Phe dipeptide self-assembly: Clues to amyloid formation
Biophysical Journal 92, 1732-41 (2007)

39- Sabaté, R.; Baxa, U.; Benkemoun, N.; de Groot; N.S.; Coulary-Salin, B.; Maddelein, M.; Malato, L.; Ventura, S.; Steven, A.C. and Saupe, S.J.
Prion and Non-prion Amyloids of the HET-s Prion forming Domain.
Journal of Molecular Biology 370, 768–783 (2007)

 38- Conchillo-Sole, O., de Groot,NS., Aviles, FX., Vendrell, J., Daura, X., and Ventura, S.
AGGRESCAN: a server for the prediction and evaluation of hot spots of aggregation in polypeptides.
BMC Bioinformatics 8:65 (2007)

37- Morell, M., de Groot, N.S. and Ventura, S.
From dust balls to biocatalysts: A new view of bacterial inclusion bodies.
Bioforum Europe. 2007, 4, 2-4 (2007)


36- de Groot, N.S. and Ventura, S.
Effect of Temperature on Protein Quality in Bacterial Inclusion Bodies
FEBS Letters 580, 6471-6476 (2006)

35- Liepina, I., Ventura, S., Czaplewskic, C. and Liwo, A.
Molecular dynamics study of amyloid formation of two Abl-SH3 domain peptides
Journal of Peptide Science 12, 780-789 (2006).

34- Gonzalez-Montalban, N., Garcia-Fruitos, E., Ventura, S, Aris, A. and Villaverde, A.
The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.
Microbial Cell Factories
5:26 (2006).

33- Ventura, S. Fernández-Escamilla, A.M., Serrano, L. and Jiménez M.A.
Design and NMR conformational study of a β-sheet peptide based on Betanova and WW domains
Protein Science
15, 2278-89 (2006).

32- Arolas, J.L, Bronsoms, S., Ventura, S., Aviles, and Calvete, J.J.
Characterizing the tick carboxypeptidase inhibitor: molecular basis for its two-domain nature
Journal of Biological Chemistry 32, 22906-22916 (2006)

31- Arolas, J.L, Aviles, F.X. Chang, J.Y. and Ventura, S.
Folding of small disulfide-rich proteins: clarifying the puzzle
Trends in Biochemical Sciences 31, 293-301 (2006)

30- de Groot, N.S. and Ventura, S.
Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
Journal of Biotechnology 125, 110-3 (2006)

29- Ventura, S. & Villaverde, A.
Protein quality in bacterial inclusion bodies
Trends in Biotechnology 24, 179-185 (2006)

28- S. de Groot, Aviles, F.X., Vendrell, J. & Ventura, S.
Mutagenesis of the central hydrophobic cluster of in Abeta42 Alzheimer’s peptide
FEBS Journal 273, 658-668 (2006)


27- S. de Groot, N. Pallares, I. Aviles, F.X., Vendrell, J. & Ventura, S.
Prediction of “hot spots” of aggregation in disease-linked polypeptides
BMC Structural Biology 5:18 (2005)

26- S. de Groot, N. & Ventura, S.
Amyloid fibril formation by bovine cytochrome c
Spectroscopy-An International Journal 19, 199-205 (2005)

25- Arolas, J.L.; Popowicz, G.M.; Bronsoms, S.; Aviles, F.X.; Huber, R.; Holak, T.A. & Ventura, S.
Study of a Major Intermediate in the Oxidative Folding of Leech Carboxypeptidase Inhibitor: Contribution of the Fourth Disulfide Bond
Journal of Molecular Biology 352, 961-75 (2005)

24- García-Castellanos, R.; Bonet-Figueredo, R.; Pallarés, I; Ventura, S.; Avilés, F.X.; Vendrell, J. & Gomis-Rüth, F.X.;
Detailed molecular comparison of the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the endogenous inhibitor latexin.
Cellular and Molecular Life Sciences 62,1996-2014 (2005)

23- García-Fruitós, E.; Gonzalez-Montalban, N.; Morell, M.; Vera, A.; Ferraz, R.M.; Arís, A.; Ventura, S. & Villaverde, A.
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins.
Microbial Cell Factories 4, 27 (2005).

22- Arolas, J.L.; D’Silva, L; Popowicz. G.M.; Aviles, F.X.; Holak, T.A.; & Ventura, S.
NMR Structural Characterization and Computational Predictions of the Major Intermediate in the Oxidative Folding of Leech Carboxypeptidase Inhibitor
Structure 13, 1193-1202 (2005)

21- Pallares, I.; Bonet, R.; Garcia-Castellanos, R.; Ventura, S.; Aviles, F.X.; Vendrell, J. & Gomis-Ruth, F.X.
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin
Proc. Natl. Acad. Sci. U S A. 102, 3978-83 (2005)

20- Carrio, M.; Gonzalez-Montalban, N.; Vera, A.; Villaverde, A. & Ventura, S.
Amyloid-like properties of bacterial inclusion bodies
Journal of Molecular Biology 347,1025-37 (2005)

19- Ventura, S.
Sequence determinants of protein aggregation: tools to increase protein solubility
Microbial Cell Factories 4,11 (2005)


18- Pallares, I.; Vendrell, J.; Aviles, F.X. & Ventura, S.
Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin.
Journal of Molecular Biology 342, 321-31 (2004)

17- Arolas, J.L.; Bronsoms, S.; Lorenzo, J.; Aviles, F.X.; Chang, J.Y. & Ventura, S.
Role of kinetic intermediates in the folding of leech carboxypeptidase inhibitor.
Journal of Biological Chemistry 279, 37261-70 (2004)

16- Arolas, J.L.; Lorenzo, J.; Rovira, A.; Vendrell, J.; Aviles, F.X. & Ventura, S.
Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties.
Biochemistry 43, 7973-82 (2004)

15- Ventura, S.; Zurdo, J.; Narayanan, S.; Parreno, M.; Mangues, R.; Reif, B.; Chiti, F.; Giannoni, E.; Dobson, C.M.; Aviles, F.X. & Serrano, L.
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.
Proc. Natl. Acad. Sci. U S A 101, 7258-63 (2004)

14- Ventura, S. & Serrano, L.
Designing proteins from the inside out.
Proteins-Structure Function and Bioinformatics 56,1-10 (2004)


We are permanently looking for post-docs with experience in biophysics, molecular biology, cell-biology and/or bioinformatics. Previous work in the field of protein folding, aggregation and protein-protein interactions is a significant plus.

Applications of students interested in doing the PhD or Master Degree in the above mentioned areas of research are wellcomed.

Please contact for details.