MRI: Acquisition of a Mass Spectrometer to Enable Research and Education at the Interface of Chemistry, Biology, and Materials Science

University Of Pittsburgh, Pittsburgh PA

Investigators

Abstract

With this award from the Major Research Instrumentation (MRI) and Chemistry Research Instrumentation and Facilities (CRIF) programs, Professor William Horne from the University of Pittsburgh and colleagues Tara Meyer and Alexander Deiters have acquired a matrix assisted laser desorption/ionization time-of-flight mass spectrometer (MALDI-TOF/TOF MS). In general, mass spectrometry is one of the key analytical methods used to identify and characterize small quantities of chemical species embedded in complex matrices. A laser impinging on the inert matrix embedded with the sample, vaporizes and ionizes the sample. The ions pass into the mass spectrometer where the masses of the parent ion and its fragment ions are measured. In a time-of-flight instrument the ions are accelerated by an electric field to allow further characterization. MALDI TOF combines gentle ionization (ideal for producing intact ions of peptides, proteins, nucleic acids, carbohydrates, synthetic polymers, and other similarly sized species) with a detection mode that offers an excellent balance between sensitivity and accuracy across a wide mass range. This highly sensitive technique allows identification and determination of the structure of molecules in a complex mixture. The acquisition strengthens the research infrastructure at the University and regional area. The instrument broadens participation by involving diverse students in research and research training with this modern analytical technique. The award is aimed at enhancing research and education at all levels, especially in areas such as (a) constructing structurally defined supramolecular biomaterials; (b) developing strategies for designing biostable mimics of complex protein folding patterns; (c) providing insights into the fundamental role of sequence in dictating polymer properties; (d) searching for approaches for small-molecule regulation of synthetic oligonucleotides in biological systems and (e) developing methods for site-specific protein mutagenesis that expand beyond the 20 canonical amino acids.