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Toxic Proteins Group
Bioquímica y Biología Molecular I
Faculty of Chemical Science
The group is not organized as a symphonic orchestra where a conductor instructs everybody about what to do and how to do it. We are more like a jazz band where any individual rules within a fixed and general framework of action. This mode of function is especially useful in our case since the hard core of the group is made of four senior scientists who have already been working together for at least 20 years. Accordingly, the scientists working in our group receive a multidisciplinary and multifaceted education and coexist with different points of view and distinct ways of making research. Debate and results discussions are frequent. Everybody works full-time without spending time in other tasks besides teaching, research or outreach science activities. This favors a scientific rich environment for postdocs, graduate and undergraduate students. Along with this same idea, we receive and train a large variety of students along the development of the academic courses. Many of them are Spanish, but many other ones come from many different countries like Italy, Germany, Portugal, USA, UK or Egypt, for example, citing only the last incorporations. They attend to our laboratory within the framework of programs such as the Erasmus-Socrates or Leonardo Da Vinci. Consequently, along this time we have supplied a great deal of laboratories, universities and pharmaceutical companies (in Spain and abroad) with workers and students who were trained in our laboratory. The group maintains a good number of national and international collaborations which involve a highly favorable multidisciplinary approach.
Our group has been studying the mechanisms of action of different toxic proteins in order to be able to turn them into treatments. With this aim, we work along three different lines of research:
1.- Turning fungal ribotoxins into highly specific antitumoral agents. Ribotoxins are toxic extracellular fungal RNases that exert highly specific activity at the larger molecule of rRNA, leading to protein biosynthesis inhibition and cell death by apoptosis. Chimeric proteins made of antibody segments and ribotoxins have been revealed as highly specific, safe and effective antitumoral agents. The aim is to keep on producing more effective but safer immunotoxins directed against different tumoral markers.
2.- Turning fungal ribotoxins into insecticidal agents. We have evidences that ribotoxins natural biological action is to defend fungi against the attack of different arthropods and we are currently taking advantage of this feature to turn them into effective and environmentally friendly insecticidal agents.
3.- Sea anemone actinoporins as a model to study the water-membrane transition of proteins. In water solution, actinoporins remain mostly monomeric and stably folded but, upon interaction with lipid membranes of specific composition, they become oligomeric integral membrane structures. Thus, this family of proteins represents an optimal system to study the transition from a soluble monomeric folded conformation to an oligomeric transmembrane protein. Actinoporins demonstrate how an identical amino acid sequence can fold into two different structures, showing the environmental influence on the energy landscape of a protein. This research pursues to understand these complex phenomena focusing not only on the proteins behavior but also on the composition and biophysics of the membrane.
Chemistry (CHE), Life Sciences (LIF)
Brief Curriculum vitae and three reference letters from three different scientists who know the applicant.
2017-07-15
Avda. Complutense, s/n; Ciudad Universitaria; 28040 - MADRID