Acquisition of a Quadrupole-Time-of-Flight Mass Spectrometer

University Of California-Santa Barbara, Santa Barbara CA

Investigators

Abstract

Mass spectrometry has recently become one of the most powerful techniques for structural characterization of biological molecules, including peptides, proteins and nucleic acids. Tandem mass spectrometry is particularly useful for sequencing these molecules, especially when only small amounts of material are available. The quadrupole time-of-flight tandem mass spectrometer will be used for routine fragmentation and unequivocal daughter fragment identification and characterization. Specific projects which will use this instrumentation include 1) investigations of the molecular mechanisms of iron acquisition by marine microorganisms in order to understand the role of iron in regulating the global carbon cycle and climate change; 2) the search for biological molecular markers of autism, 3) the synthesis and characterization of polymeric peptide adhesives with industrial and medical applications, 4) the development biological nanofabrication processes of new high performance composites and 5) investigations of amphiphilic peptides to control the cell response, particularly on biologically active material surfaces. The quadrupole time-of flight mass spectrometer will include a high pressure liquid chromatograph to separate compounds before analyzing their masses and fragmentation patterns. The mass spectrometer will consist of a quadrupole as the first mass analyzer, followed by a quadrupole collision cell and a time-of-flight detector as the second mass analyzer. The system will also be configured with nanospray and micro ion spray capabilities to allow for a range of flow rates and to permit the small amounts of biological samples to be analyzed. The system will use electrospray ionization (ESI) for soft ionization of proteins and peptides or atmospheric pressure chemical ionization (APCI) for analysis of polar organic molecules. The quadrupole time-of flight mass spectrometer will significantly enhancing the research infrastructure at the University of California, Santa Barbara by extending the mass range and sensitivity capabilities of the UCSB Mass Spectrometry Facility which is housed in the Department of Chemistry and Biochemistry. For example, this instrument provides the capability to elucidate the structures of peptides, proteins and nucleic acids, which is required by the research groups that will use this instrumentation. This mass spectrometer will also significantly enhance student training, by providing exposure to and training in modern structure determination methodologies, which will certainly be useful in the emerging areas of proteomics, genomics and bioinformatics.