Abstract

The overall objective of the proposed research continues to be to develop and use mass spectrometry as a tool for solving problems of biomedical interest, especially those dealing with the characterization of complex polar compounds and others of high molecular weight. The powerful research mass spectrometers--a VG 70-SE4F and a VG ZAB-SE--will be used in assigning structures to complex peptides and proteins: aldose reductases, cytochromes, marine-derived toxins, insect and marine invertebrate neuropeptides, marine algal and cyanobacterial GABA-mimetic peptides, and peptide antibiotics. The instruments will also be employed in improving or developing the FAB technique: by improving high-resolution FAB; by enhancing ion production with laser assistance; developing LC/HRMS and LC/MS/MS; and by applying LC/FAB to gradient elution HPLC and countercurrent chromatography (CCC). The mass spectrometric techniques developed will be applied to solving structural problems of the P.I. (antiviral and antitumor agents from marine sources, antibiotics, marine-derived chlorins, cyanobacterial toxins, a hibernation factor in bears' blood, hydroxamates from Hemophilus influenzae) and other biomedical scientists at the University of Illinois (i.a., methanogen cofactors, metallo-porphyrins, estrogen receptors, fluorinated steroids, viral proteins, phospholipids, glycolipids, and glycosphingolipids).

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM027029-22
Application #
3274489
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1979-05-01
Project End
1995-07-31
Budget Start
1993-08-01
Budget End
1994-07-31
Support Year
22
Fiscal Year
1993
Total Cost
Indirect Cost

  Institution

Name
University of Illinois Urbana-Champaign
Department
Type
Schools of Arts and Sciences
DUNS #
041544081
City
Champaign
State
IL
Country
United States
Zip Code
61820

  Publications

Schmidt, Joann; Kuhlenschmidt, Mark S (2008) Microbial adhesion of Cryptosporidium parvum: identification of a colostrum-derived inhibitory lipid. Mol Biochem Parasitol 162:32-9
Kim, Sung Hoon; Katzenellenbogen, John A (2006) Hormone-PAMAM dendrimer conjugates: polymer dynamics and tether structure affect ligand access to receptors. Angew Chem Int Ed Engl 45:7243-8
Baggett, Scott; Protiva, Petr; Mazzola, Eugene P et al. (2005) Bioactive benzophenones from Garcinia xanthochymus fruits. J Nat Prod 68:354-60
Zhou, Hai-Bing; Comninos, John S; Stossi, Fabio et al. (2005) Synthesis and evaluation of estrogen receptor ligands with bridged oxabicyclic cores containing a diarylethylene motif: estrogen antagonists of unusual structure. J Med Chem 48:7261-74
Yang, Hui; Protiva, Petr; Gil, Roberto R et al. (2005) Antioxidant and cytotoxic isoprenylated coumarins from Mammea americana. Planta Med 71:852-60
De Angelis, Meri; Stossi, Fabio; Carlson, Kathryn A et al. (2005) Indazole estrogens: highly selective ligands for the estrogen receptor beta. J Med Chem 48:1132-44
Bigott, Heather M; Parent, Ephraim; Luyt, Leonard G et al. (2005) Design and synthesis of functionalized cyclopentadienyl tricarbonylmetal complexes for technetium-94m PET imaging of estrogen receptors. Bioconjug Chem 16:255-64
De Angelis, Meri; Stossi, Fabio; Waibel, Michael et al. (2005) Isocoumarins as estrogen receptor beta selective ligands: Isomers of isoflavone phytoestrogens and their metabolites. Bioorg Med Chem 13:6529-42
De Angelis, Meri; Katzenellenbogen, John A (2004) Ring nitrogen-substituted non-steroidal estrogens: pyridine and pyrimidine analogs of the phenol in deoxyhexestrol experience resonance constraints on preferred ligand conformation. Bioorg Med Chem Lett 14:5835-9
Sivaraman, Sharada; Sullivan, Todd J; Johnson, Francis et al. (2004) Inhibition of the bacterial enoyl reductase FabI by triclosan: a structure-reactivity analysis of FabI inhibition by triclosan analogues. J Med Chem 47:509-18

Showing the most recent 10 out of 125 publications