Tim Aguirre

RESEARCH:

I was always intrigued by the complexity of biological processes and wanted to use my chemistry background to interrogate biological systems. Studying kinase inhibitors for therapeutically relevant targets during my PhD was intriguing and helped me gain profound knowledge about kinase signaling and small molecule inhibitors. For my postdoctoral studies, I will focus on the ubiquitin machinery and develop synthetic ubiquitin probes as baits for mass spectrometry-based proteomics. Ubiquitylation is a multifaceted post-translational modification involved in a cornucopia of biological processes and identifying novel endogenous writers, readers and erasers of unconventionally linked ubiquitin chains will contribute to a better understanding of the complex ubiquitin code. Revealing cellular functions and disease pathways regulated by unique ubiquitin linkages could be a springboard for therapeutic intervention in the long run.

CURRICULUM VITAE:

I studied chemistry at the Humboldt University Berlin, where I obtained my Bachelor’s degree in 2016.  For my Bachelor’s thesis and a subsequent research internship at the University of Warwick (UK), I investigated different types of peptide-polymer conjugates for diverse applications such as fiber-reinforced composites or anti-microbials. I then changed to the chemical biology field and implemented the analog-sensitive approach to inositol hexakisphosphate kinases for my Master’s degree, which I completed in 2018.

I stayed in the same lab for my PhD studies and further interrogated the inositol pyrophosphate metabolism by identifying selective kinase inhibitors using chemical genetics and high-throughput screening. In addition, I used photopharmacology to target T. gondii calcium-dependent protein kinase 1 in a reversible and time-dependent manner.

In October 2023, I started as a Walter Benjamin postdoctoral researcher at the LUMC under the joint supervision of Gerbrand van der Heden van Noort and Alfred Vertegaal. My aim is to investigate oxyester-linked ubiquitin chains employing chemically synthesized diubiquitin probes and mass spectrometry-based proteomics.