IBB UAB

Author: Nati Infante

Dr. Antoni Villaverde: Self-assembling toxin-based nanoparticles as self-delivered antitumoral drugs

Dr. Antoni Villaverde: Self-assembling toxin-based nanoparticles as self-delivered antitumoral drugs

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https://www.sciencedirect.com/science/article/pii/S016836591830049X     Abstract Loading capacity and drug leakage from vehicles during circulation in blood is a major concern when developing nanoparticle-based cell-targeted cytotoxics. To circumvent this potential issue it would be convenient the engineering of drugs as self-delivered nanoscale entities, devoid of any heterologous carriers. In this context, we have here engineered potent protein toxins, namely segments of the diphtheria toxin and the Pseudomonas aeruginosa exotoxin as self-assembling, self-delivered therapeutic materials targeted to CXCR4+ cancer stem cells. The systemic administration of both nanostructured drugs in a colorectal cancer xenograft mouse model promotes efficient and specific local destruction of targe
Dr. A. Villaverde: Improving Biomaterials Imaging for Nanotechnology: Rapid Methods for Protein Localization at Ultrastructural Level

Dr. A. Villaverde: Improving Biomaterials Imaging for Nanotechnology: Rapid Methods for Protein Localization at Ultrastructural Level

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http://onlinelibrary.wiley.com/doi/10.1002/biot.201700388/full Abstract The preparation of biological samples for electron microscopy is material- and time-consuming because it is often based on long protocols that also may produce artifacts. Protein labeling for transmission electron microscopy (TEM) is such an example, taking several days. However, for protein-based nanotechnology, high resolution imaging techniques are unique and crucial tools for studying the spatial distribution of these molecules, either alone or as components of biomaterials. In this paper, we tested two new short methods of immunolocalization for TEM, and compared them with a standard protocol in qualitative and quantitative approaches by using four protein-based nanoparticles. We reported a significant increas...
Dr. David Reverter: Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase

Dr. David Reverter: Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase

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https://www.sciencedirect.com/science/article/pii/S0969212617304033?via%3Dihub Summary Lipases and esterases constitute a group of enzymes that catalyze the hydrolysis or synthesis of ester bonds. A major biotechnological interest corresponds to thermophilic esterases, due to their intrinsic stability at high temperatures. The Pf2001 esterase from Pyrococcus furiosus reaches its optimal activity between 70°C and 80°C. The crystal structure of the Pf2001 esterase shows two different conformations: monomer and dimer. The structures reveal important rearrangements in the “cap” subdomain between monomer and dimer, by the formation of an extensive intertwined helical interface. Moreover, the dimer interface is essential for the formation of the hydrophobic channel for substrate selectivity,
Dr. Antoni Villaverde: Protein nanoparticles are nontoxic, tuneable cell stressors

Dr. Antoni Villaverde: Protein nanoparticles are nontoxic, tuneable cell stressors

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  Protein nanoparticles are nontoxic, tuneable cell stressors   Aim: Nanoparticle–cell interactions can promote cell toxicity and stimulate particular behavioral patterns, but cell responses to protein nanomaterials have been poorly studied. Results: By repositioning oligomerization domains in a simple, modular self-assembling protein platform, we have generated closely related but distinguishable homomeric nanoparticles. Composed by building blocks with modular domains arranged in different order, they share amino acid composition. These materials, once exposed to cultured cells, are differentially internalized in absence of toxicity and trigger distinctive cell adaptive responses, monitored by the emission of tubular filopodia and enhanced drug sensitivity. Conc
Dr. Antoni Villaverde: Improving biomaterials imaging for nanotechnology: rapid methods for protein localization at ultrastructural level

Dr. Antoni Villaverde: Improving biomaterials imaging for nanotechnology: rapid methods for protein localization at ultrastructural level

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  Improving biomaterials imaging for nanotechnology: rapid methods for protein localization at ultrastructural level http://onlinelibrary.wiley.com/doi/10.1002/biot.201700388/full Abstract The preparation of biological samples for electron microscopy is material- and time-consuming because it is often based on long protocols that also may produce artifacts. Protein labeling for transmission electron microscopy (TEM) is such an example, taking several days. However, for protein-based nanotechnology, high resolution imaging techniques are unique and crucial tools for studying the spatial distribution of these molecules, either alone or as components of biomaterials. In this paper, we tested 2 new short methods of immunolocalization for TEM, and compared them with a standard pr...