David Mascotti, Ph.D.
Professor
Background
Dr. Mascotti joined the faculty in the summer of 1998. He completed his Ph.D. in 1992 studying nucleic acid chemistry and the interactions of synthetic peptides (that served as simpler models of proteins) with DNA and RNA. After completing his Ph.D., Dr. Mascotti accepted a National Institutes of Health Postdoctoral Fellowship to work at Washington University in St. Louis. While there, he studied iron metabolism and the control mechanisms of ferritin synthesis. After his postdoctoral work, he was an assistant professor at the Richard Stockton College of New Jersey for two years. He now teaches general chemistry, biochemistry, and is a Faculty Fellow in Entrepreneurship at JCU where he has taught courses as part of the Entrepreneurship Minor. He also served as Chemistry Department Chair from 2005-2009.
Areas of Expertise
- Biochemistry
Research Interests
The Mascotti lab studies several biochemical processes such as protein-nucleic acid interactions, gene expression, and oxidative damage control. Toward understanding protein-nucleic acid interactions, we study the thermodynamic effects of small molecule redistribution that accompanies these macromolecular binding events. These interactions are central to gene expression at the replication, transcription, and translational levels. Also, somewhat surprisingly, at least one enzyme involved in cellular antioxidant defenses interacts with DNA and RNA which leads back to protein-nucleic acid interactions.
Oxidative Damage Control. Reactive radicals are commonly the culprits of biological damage leading to, but not limited to, cardiovascular damage, strokes, cancer, Alzheimer’s disease, autism, and diabetic neuropathy. Exogenous small molecule antioxidants (reductants in chemical terms) such as Vitamins C and E act to “mop up” the radicals as gratuitious scavengers. Endogenous small molecules such as glutathione perform similar scavenging ability. Endogenous enzymes such as superoxide dismutase and catalase are the heart of most organisms’ antioxidant defenses who live in an oxygenated environment. We primarily focus on the enzyme superoxide dismutase in our lab, particularly with regard to its ability to bind DNA and RNA in the mitochondria.
Protein-nucleic acid interactions. A major force governing these interactions is the redistribution of small molecules that accompanies the macromolecular binding. These "Lilliputian" effects can be quite significant, and are one of my current interests. These studies involve equilibrium binding studies and structural studies of peptide- or protein-RNA or -DNA interactions. The proteins under study include the interaction of both bacterial and mitochondrial Superoxide Dismutases with DNA and RNA. We currently use techniques like fluorescence spectroscopy, UV/Vis spectroscopy, nitrocellulose filter binding assays and electromobility shift assays.
Gene expression (particularly translational regulation). Expression of proteins can be regulated at several points. Most commonly, transcription and translation are regulated, however post-transcriptional events such as mRNA stability is coupled to translation regulation via miRNA, siRNA, RNAi, shRNA, did I miss any? We are working on ways to create, package, and deliver these regulatory RNA molecules into cells for therapeutic purposes.
Education
B.S., Hope College, MI
Ph.D. (Biochemistry), Texas A&M University
Post-Doctoral Research Assistant, Department of Biology, Washington Univ.- St. Louis, 1992-1996
Assistant Professor, Chemistry Program, Richard Stockton College of New Jersey, 1996-1998
Assistant Professor, Chemistry Department, John Carroll University
Courses Taught
- General Chemistry (CH141, CH142)
- Biochemistry and Lab (CH435, CH436, CH437, CH439)
- STEMM Entrepreneurship
- Introduction to Entrepreneurship
- Informed Health Decisions (link to Entrepreneurship
- Intro to Pharmacy
Publications
Research Papers
19- Waner, MJ, Ellis, G, Graeca, M, Ieraci, N, Morell, C, Murphy, A, and Mascotti, DP, 2023. “Avidin Cooperative Allosterism upon Binding Biotin Observed by Differential Changes in Intrinsic Fluorescence” Biochem. Biophys. Reports. 36. p. 101554
18- Waner, MJ, Hiznay, JM, Mustovich, AT, Patton, W, Ponyik, C and Mascotti, DP. 2019. "Streptavidin cooperative allosterism upon binding biotin observed by differential changes in intrinsic fluorescence". Biochem. Biophys. Reports. 17. pp. 127-131. (online link)
17- Savasky, BM, Mascotti, DP, Patel, N, & Rodriguez-Collazo, E. 2018. "Nutrition and Pharmacological Effects on Oxidative Stress in Soft Tissue and Bone Remodeling " J. Nutr. Metab. 2018. 9 pages (online link)
16- Smolik, A.C., Bengez-Pudja, L. & Cheng, I. & Mascotti, D.P. 2014. Characterization of E. coli Manganese Superoxide Dismutase Binding to RNA and DNA." Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1844(12): 2251-2256. (.pdf copy)
15-David P. Mascotti & Mark J. Waner. 2010. Complementary Spectroscopic Assays for Investigating Protein-Ligand Binding: a Project for the Advanced Chemistry Laboratory . Journal of Chemical Education 87.7: 735-38.
14- Lissemore, J.L., Bayes. J., Calvey, M., Reineke, L., Colagiavanni, A., Tscheiner, M., and Mascotti, D.P. Molecular Biology Reports. 2008 "Green Fluorescent Protein is Superior to Blue Fluorescent Protein as a Quantitative Reporter of Relative Promoter Activity in E. coli."Mol Biol Rep. [2008 Jul 13. Epub ahead of print].
13- Waner, M.J. & Mascotti, D.P. 2008. A Simple Spectrophotometric Streptavidin-Biotin Binding Assay Utilizing Biotin-4-Fluorescein. J. Biochem. Biophys. Meth. 70: 873-877.
12- Czerwinski, J.D. Hovan, S.C. & Mascotti, D.P. 2005. Quantitative Non-Isotopic Nitrocellulose Filter Binding Assays: Bacterial MnSOD-DNA Interactions. Anal Biochem. 336:300-4. (.pdf copy)
11- Waner, M.J., Navrotskaya, I., Bain, A., Oldham, E.D., & Mascotti, D.P. 2004. Thermal and Sodium Dodecylsulfate Induced Transitions of Streptavidin. Biophys. J.87:2701-2713. (.pdf copy)
10- Lissemore, J.L., Jankowski, J.T., Thomas, C.B., Mascotti, D.P., and deHaseth, P.L., 2000. Green Fluorescent Protein as a Quantitative Reporter of Relative Promoter Activity in E. coli. Biotechniques 28: 82-89. (.pdf copy)
9- Rodgers, J.T., Patel, P., Hennes, J.L., Bolognia, S.L. & Mascotti, D.P., 2000. Use of Biotin-labeled RNA for Protein Purification and Agarose-based Chemiluminescent Electromobility Shift Assays. Analyt. Biochem. 277: 254-259. (.pdf copy)
8- Goessling, L.S. Mascotti, D.P. & Thach, R.E., 1998. Involvement of Heme in the Degradation of Iron-regulatory Protein 2. J. Biol. Chem. 273: 12555-12557. (.pdf copy)
7- Mascotti, D.P. & Lohman, T.M., 1997. Thermodynamics of Oligoarginines Binding to RNA and DNA. Biochemistry 36: 7272-7279. (.pdf copy)
6- Mascotti, D.P. & Lohman, T.M., 1995. Thermodynamics of Heparin-Charged Oligopeptide Interactions. Biochemistry 34: 2908-2915. (pubmed entry)
5- Goessling, L.S., Mascotti, D.P., Bhattacharyya, M., Gang, H. & Thach, R.E., 1994. Irreversible Steps in the Ferritin Synthesis Induction Pathway. J. Biol. Chem. 269: 4343-4348. (.pdf copy)
4- Mascotti, D.P. & Lohman, T.M., 1993. Thermodynamics of Single Stranded Nucleic RNA and DNA Interactions with Oligolysines Containing Tryptophan: Effects of Base Composition. Biochemistry 32: 10568-10579. (pubmed entry)
3- Mascotti, D.P. & Lohman, T.M., 1992. Thermodynamics of Single Stranded RNA Binding to Oligolysines Containing Tryptophan. Biochemistry 31: 8932-8946. (pubmed entry)
2- Mascotti, D.P. & Lohman, T.M., 1990. Thermodynamic Extent of Counterion Release upon Binding Oligolysines to Single-Stranded Nucleic Acids. Proc. Nat. Acad. Sci. 87: 3142- 3146. (.pdf copy)
1- Boyer, R.F., Mascotti, D.P. & Schori, B.E., 1986. Ferroxidase Activity of Mushroom Tyrosinase. Phytochemistry 25: 1281-1283.
Review Articles
6- Mascotti, D.P. 2010. Control of Iron Metabolism. In Principles of Medical Biology, eds. E.E. Bittar & N. Bittar, in press. Greenwich, CT: JAI Press.
5- Mascotti, D.P., Goessling, L.S., Rup, D. & Thach, R.E. 1998. Mechanisms for Induction and Rerepression of Ferritin Synthesis. In Metal Ions in Gene Regulation, eds. S. Silver & W.E. Walden, pp. 217-230. New York: Chapman & Hall
4- Mascotti, D.P., Daniels-McQueen, S., Goessling, L.S., Rup, D. & Thach, R.E. 1996. Effects of the Ferritin Open Reading Frame on Translation Induction by Iron. Prog. Nuc. Acids Molec. Biol. 55: 121-133.
3- Mascotti, D.P., Rup, D. & Thach, R.E. 1995. Regulation of Iron Metabolism: Translational Effects Mediated by Iron, Heme and Cytokines. Ann. Rev. Nutr. 15: 239-261. (pubmed entry)
2- Lohman, T.M. & Mascotti, D.P., 1992. Thermodynamics of Ligand-Nucleic Acid Interactions. Meth. Enzymol. 212: 400-424. (.pdf copy)
1- Lohman, T.M. & Mascotti, D.P., 1992. Non-Specific Ligand-DNA Equilibrium Binding Parameters Determined by Fluorescence Methods. Meth. Enzymol. 212: 424-458.
