Author: Nati Infante

                   

  SWI (Small World Initiative) és un projecte participatiu internacional (Yale University, EUA, 2012) dirigit a la comunitat educativa per a l'exploració de la diversitat microbiana en els sòls per descobrir microorganismes productors de nous antibiòtics. A la UAB aquest programa el lidera i coordina la Dra. Montserrat Llagostera de la Unitat de Microbiologia Campus del Departament de Genètica i de Microbiologia. Al IBB els SWI Partner Instructors (SWIPI) són Isidre Gibert, Daniel Yero i Oscar Conchillo del grup de Genètica Molecular i Patogènesi Bacteriana que condueixen a 12 SWI Technical Assitants (SWITAs), estudiants de darrer curs dels graus de Microbiologia, Genètica, Biotecnologia i Biologia.   SWI-UAB està present a la xarxa a traves de:           Web: http://pagine

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

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...

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,