Graduate Faculty Directory
Catherine Bentzley
Department of Chemistry & Biochemistry
Education
- BS (St. Joseph’s University)
- PhD (University of Delaware)
Faculty Appointments
Associate Professor of Chemistry
Synopsis
The rapid and enormous expansion in the biotechnology revolution has caused increased interest in determining exact molecular weights of biological systems. Mass spectrometry offers a quick and convenient method for determining accurate molecular weights of biological samples including peptides, proteins, oligonucleotides and oligosaccharides. Matrix-Assisted Laser Desorption Ionization (MALDI) and Electrospray Ionization (ESI) are the two predominant mass spectrometry techniques used for the development of biological assays. During the MALDI process singly charged analyte ions are produced after desorption/ionization from a matrix using a nitrogen laser. For example, in our laboratory we utilize MALDI to detect amiodarone, an anti-arrhythmic drug, in biopsies of explanted human hearts from cardiac transplant recipients. In another study MALDI is used to track the decomposition of PCR primers over various periods of time ranging from 1 day to 10 years. In contrast to MALDI, the ESI method ionizes an analyte to form charged species through desolvation of microscopic droplets. A resultant ESI spectrum contains a multiply protonated envelope of various mass-to-charge ratios. ESI can be used to track the activity of protein kinases as well as the modulation of the kinase activity. To demonstrate the effectiveness of using ESI-MS as a kinase assay, one of the best-characterized kinases, cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) is studied. ESI can also be utilized to study the conformational changes of protein structures as they undergo desolvation. It is also possible to analyze the denaturing of oligonucleotide strands as the sample enters the gaseous phase.Publications & Presentations
- “Secondary Structural Characterization of Oligonucleotide Strands Using Electrospray Ionization Mass Spectrometry,” X. Guo, M. F. Bruist, D. L.Davis, and C. M. Bentzley,” Nucleic Acid Research, 2005, 33, 3659.
- “Quantitation of Underivatized Free Amino Acids in Mammalian Cell Culture Media Using Matrix Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry,” J. Dally, J. Gorniak, R. Bowie, and C. Bentzley, Anal. Chem., 2003, 75(19), 5046.
- “Analysis of the Degradation of Oligonucleotide Strands during the Freezing/Thawing Processes Using MALDI-MS,” D. L. Davis, E. O’Brien, and C. M. Bentzley, Anal. Chem., 2000, 20, 5092.
- “Identification of Overhangs in Double Stranded DNA by Enzymatic Digestion with MALDI Analysis,” W. Bartolini, C. M. Bentzley, M. V. Johnston, and B. S. Larsen, J. Am. Soc. Mass. Spectrometry, 1999, 10, 521.
- “Base Specificity of Oligonucleotide Digestion by Calf Spleen Phosphodiesterase with Matrix-Assisted Laser Desorption Ionization Analysis,” C. M. Bentzley, M. V. Johnston, and B. S. Larsen, Anal. Biochem.,1998, 258, 31.
Contact Information
Office:
Griffith Hall
Room # 240
Box # 48
Phone: 215.596.8581
Email: c.bentzl@usp.edu
