Juan M. Ruso, Associate Professor
Soft Matter and Molecular Biophysics Group
Department of Applied Physics
University of Santiago de Compostela (USC)
E-15782 Santiago de Compostela. Spain
Phone: (+34) 981 563 100 ext. 14042
Fax: (+34) 981 520 676
E-mail: JuanM.Ruso at usc.es
My research is centered on two topics, the synthesis and characterization of nanostructured templated materials and the biophysics of proteins and ligand-protein interactions. On the first topic, by bringing together my expertise in molecular self-assembly, interfacial phenomena or rheology, the effort is to design and measure functional materials with controlled composition and architecture on multiple length scales to achieve desirable properties and applications at a macroscopic level. In most cases, the self-assembly structure is strongly affected by the inorganic precursor so the mechanism is a much more complex where synergist effect can be tailored to create new perspectives. This exciting and rewarding area of study has potential applications as ceramics, molecular sieves, catalyst supports, photonics, sensors and imaging, tissue engineering, microvascular networks or dr ug design and delivery.
SEM microphotographs of SiO2 materials templated with microelumsion
|SEM microphotographs of TiO2 templated with microelumsion||Anatase nanoparticles|
On the second topic, I have studied the complexation of different proteins with amphiphilic ligands (surfactants, lipids and drugs). The interactions between small molecules with proteins affect their respective biological functions and determine their stability in solution with respect to aggregation, liquefaction, and other phase transformations. Furthermore, the pathways of protein aggregation, crystal formation, folding, or unfolding are largely defined by the forces acting between the molecules. The understanding of molecular recognition in protein–ligand complexes is crucial to better comprehend the associated biological function and of practical importance in the discovery, for instance, of new drugs. Elucidating the role of these interactions concomitantly with the involved time scales must provide insights and new solutions relevant to areas including protein engineering, cellular and metabolic engineering, biomolecular engineering, bionanotechnology, biosensors, biomaterials, and personalized medicine.
SAXS curves of fibrinogen
|SEM microphotograph of fibrinogen hydrogel||Gibbs energies of interaction per mol of HSA as a function of the number of sodium perfluorooctanoate (left-hand plots) and sodium dodecanoate (right-hand plots) molecules bound to the HSA molecule|