Mickey Muscalli

Mickey grew up in Baltimore, Maryland and later attended the University of Maryland Baltimore County (UMBC) for his undergraduate studies. There, he received a BS in Independent Studies with a focus on Astrobiology and Instrumental Data. Along the way, he participated in research under the direction of UMBC’s Dr. Stephen Freeland, which aimed to help simulate and better understand the parameter landscape for life’s 20 genetically encoded amino acids, as well as the landscape for the near-limitless number of potential “xeno-amino acids” which we do not observe in life on Earth. This research helped ignite an interest in one of life’s most fundamental complexifications, the transition from simple organic monomer units to more complex oligopeptides, and how this space could be explored through further experimental analysis and modeling. Mickey chose to further these studies through the RARE Center in the labs of RPI’s Prof. Karyn Rogers and Prof. Jake Shelley.

Mickey’s research at RPI has broadly focused on the mechanisms by which simple amino acids could overcome the thermodynamic barriers facing aqueous peptide synthesis under plausible prebiotic conditions. Primarily, lab analysis has focused on reproducing the so-called Salt-Induced-Peptide-Formation pathway, in which salt is used as a dehydrating agent—lowering water activity of the solution and shifting reaction equilibrium toward peptide formation. Moving forward, our work seeks to better characterize how the various parameters of this pathway (salt concentration, metal cations, temperature, pressure, etc.) contribute to its overall viability and to assess how that may better situate this mechanism in an environmental context. Moreover, we seek to further explore mechanistic pathways like this one through thermodynamic calculations and modeling efforts.