Abstract

The long-term objective of this proposal is to combine two mass spectrometry-based analytical approaches, bioreactive mass spectrometer probes and surface plasmon resonance biomolecular interaction analysis mass spectrometry, into one unified technique for biomolecular characterization (termed """"""""Biosensor Chip Mass Spectrometry""""""""). In order to accomplish this objective, it will be necessary to investigate and optimize different surface derivatization chemistries, find working combinations of enzymes/chemicals for modification of analytes, develop new analytical strategies, and perfect sample preparation techniques used during analysis. Thus, the specific aims of the proposal are to investigate these aspects of biosensor chip mass spectrometry, and in the process develop methods nd protocols needed for routine application. Initial research will investigate surface amplification chemistries and various enzyme combinations designed for protein sequence elucidation, At the same time, methods for optimizing biosensor control and mass spectrometry sample preparation will be developed. Later research will investigate various enzyme combinations designed for viewing protein higher-order structure and for analysis of post-translational modifications.

Proposed Commercial Applications

NOT AVAILABLE

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Small Business Innovation Research Grants (SBIR) - Phase I (R43)
Project #
5R43CA082079-02
Application #
6146234
Study Section
Special Emphasis Panel (ZRR1-BRT-4 (01))
Program Officer
Song, Min-Kyung H
Project Start
1998-09-30
Project End
2000-09-29
Budget Start
1999-09-30
Budget End
2000-09-29
Support Year
2
Fiscal Year
1999
Total Cost
Indirect Cost

  Institution

Name
Intrinsic Bioprobes, Inc.
Department
Type
DUNS #
965127038
City
Tempe
State
AZ
Country
United States
Zip Code
85284

  Publications

Nedelkov, Dobrin; Tubbs, Kemmons A; Nelson, Randall W (2002) Design of buffer exchange surfaces and sensor chips for biosensor chip mass spectrometry. Proteomics 2:441-6
Nedelkov, D; Nelson, R W (2001) Analysis of native proteins from biological fluids by biomolecular interaction analysis mass spectrometry (BIA/MS): exploring the limit of detection, identification of non-specific binding and detection of multi-protein complexes. Biosens Bioelectron 16:1071-8
Nedelkov, D; Nelson, R W (2001) Delineation of in vivo assembled multiprotein complexes via biomolecular interaction analysis mass spectrometry. Proteomics 1:1441-6
Nedelkov, D; Nelson, R W (2001) Analysis of human urine protein biomarkers via biomolecular interaction analysis mass spectrometry. Am J Kidney Dis 38:481-7
Nelson, R W; Nedelkov, D; Tubbs, K A (2000) Biomolecular Interaction Analysis Mass Spectometry. BIA/MS can detect and characterize protiens in complex biological fluids at the low- to subfemtomole level. Anal Chem 72:404A-411A
Bakhtiar, R; Nelson, R W (2000) Electrospray ionization and matrix-assisted laser desorption ionization mass spectrometry. Emerging technologies in biomedical sciences. Biochem Pharmacol 59:891-905
Nelson, R W; Nedelkov, D; Tubbs, K A (2000) Biosensor chip mass spectrometry: a chip-based proteomics approach. Electrophoresis 21:1155-63
Nedelkov, D; Rasooly, A; Nelson, R W (2000) Multitoxin biosensor-mass spectrometry analysis: a new approach for rapid, real-time, sensitive analysis of staphylococcal toxins in food. Int J Food Microbiol 60:13-Jan
Nedelkov, D; Nelson, R W (2000) Practical considerations in BIA/MS: optimizing the biosensor-mass spectrometry interface. J Mol Recognit 13:140-5
Nelson, R W; Krone, J R (1999) Advances in surface plasmon resonance biomolecular interaction analysis mass spectrometry (BIA/MS). J Mol Recognit 12:77-93

Showing the most recent 10 out of 11 publications