Office: Jennie Smoly Caruthers Biotech Building, Room A417
Lab: JSCBB A480 (4th floor, A wing)
Lab Phone: 303-735-6334
Ph.D.: University of Buenos Aires, 1995
Pharm. D. University of Buenos Aires, 1989
Postdoctoral Fellow: School of Medicine Stanford University, 1995-2001
Awards:New Scholar in Global Infectious Disease. The Ellison Medical Foundation (2004)Junior Faculty Development Award. University of Colorado at Boulder (2003)Scientist Development Award. American Heart Association (2003-present)
Molecular Biophysics, Proteins & Enzymology, Structural Biology
Our research program seeks to understand, in molecular detail, fundamental cellular processes that occur at the membrane interface. We utilize a multidisciplinary approach in our program. X-ray crystallography is our main tool to obtain high-resolution structures and macromolecular mechanisms are elucidated with complementary biochemical and biophysical studies including NMR, Small Angle X-Ray Scattering and EM.
Three fundamental membrane-related systems are the focus of our program:
(i) Folding and Insertion of Membrane Proteins in the Bacterial and Mitochondrial Outer Membrane: We seek to understand the molecular mechanisms by which chaperones and the BAM membrane protein complex cooperate to promote folding and specific insertion of b-barrel OMPs into bacterial and mitochondrial outer membranes.
(ii) Modification of the Bacterial Outer Membranes Mediating Antibiotic Resistance: Lipid-A modification with Ara4N confers resistance antimicrobial peptides of the innate immune system as well as antibiotics such as colistin. The focus of our research is to determine the structure and mechanism of enzymes essential for Lipid-A modification with Ara4N as a key for the design and evaluation of specific inhibitors.
(iii) Signaling Pathways at the Membrane Interface: Membrane-bound Guanylyl Cyclases: We seek to determine the molecular basis for disease causing mutations in GCs as well as validating the hypothesis of a conserved activation mechanism for all members of the membrane-GCs family.