Julio A. Camarero Associate Professor Department of Pharmacology and Pharmaceutical Sciences School of Pharmacy

Education:
B.Sc. 1990 Chemistry - University of Barcelona, Spain
Ph.D. 1996 Organic Chemistry - University of Barcelona, Spain

Postdoctoral Research Fellowship:
1996 - 2000 The Rockefeller University

Started at USC: 1997

Research Topics: Chemical Biology, Protein and peptide therapeutics, Microbial pathogenicity, Genetically-encoded Biosensors

Research Description

The practical and conceptual opportunities made available by recent innovations in the emerging fields of synthetic protein chemistry and protein expression using modified protein splicing elements are providing a fertile source for innovative biotechnology tools to study the physico-chemical basis of protein function in vivo and in vitro.

The Camarero Lab is focused in using these generic chemistry-driven technologies for studying biological process involved in bacterial pathogenicity and Chem-Biosensing. Some of the actual working projects involve:

1. Development of new methods for the biosynthesis and screening of biological libraries inside living cells for the rapid detection of small molecules able to inhibit or attenuate intracellular molecular recognition events. Our initial focus has been to produce high-affinity ligands (using highly constrained circular peptides such as cyclotides as molecular scaffolds) that can disable bacterial pathogenicity and other biological toxins, but this approach can also be easily used to find small circular peptides capable of disrupting any biomolecular interaction. For example, the method can be used to find molecules that may disrupt the destructive mechanisms involved in cancer and neurodegenerative diseases such mad cow and Alzheimer’s.
2. Development of molecular tools for the study of protein/protein interactions in real time and at single cell level. Key to this approach is the development of new molecular tools based on photomodulated protein trans-splicing that will allow the reconstitution and site-specific labeling of particular proteins inside the host cell with total temporal and spatial control. The use and development of new orthogonal split inteins is being used for the simultaneous multicolor site-specific labeling of different proteins in vivo. This approach is being used to study the pathogenicity of Yersinia pestis (the causative agent of plague) in real time and at single cell level to better understand the virulence mechanisms associated with this human pathogen
3. Rapid production of protein microarrays to understand interactions in microbial pathogenicity and how to modulate them. This project involves interfacing the method of protein immobilization that we have developed based on protein trans-splicing with high-throughput cloning and expression methods, such as Gateway-like and cell-free expression systems. This allows the rapid production of high quality protein chips of a particular proteome. Analysis and identification of the proteins captured by the microarray is carried out using mass spectrometry (MALDI MS and MALDI MS/MS). We have started to produce protein chips containing proteins from Y. pestis type III secretion system, which include cytotoxins and effectors. This approach is being used for the analysis of protein/protein interactions to study bacterial pathogenicity.