Application of mass spectrometry for target identification and characterization

Autor:	Rachel R. Ogorzalek Loo, Ping Du, Tracy I. Stevenson, Joseph A. Loo, Dana Dejohn
Rok vydání:	1999
Předmět:	Pharmacology Gel electrophoresis Chromatography Protein mass spectrometry Chemistry Isoelectric focusing Electrospray ionization Proteomics Mass spectrometry Biochemistry Drug Discovery Molecular Medicine Polyacrylamide gel electrophoresis Antibacterial agent
Zdroj:	Medicinal Research Reviews. 19:307-319
ISSN:	1098-1128 0198-6325
DOI:	10.1002/(sici)1098-1128(199907)19:4<307::aid-med4>3.0.co;2-2
Popis:	Mass spectrometry-based methodologies span the vast expanse of drug discovery. Both electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) support proteomics-based research projects by identifying proteins separated and isolated by polyacrylamide gel electrophoresis. MALDI-MS-based surface scanning of one-dimensional isoelectric focusing gels, “virtual 2-D gel electrophoresis,” represents a potentially high throughput means to map proteins and to determine protein profiles. Mass spectrometry can also be used to directly study the covalent and noncovalent interactions of drug molecules and biomolecule targets. Drug binding examples discussed include the binding of covalent and noncovalent inhibitors to src SH2 domain protein, and the interaction of aminoglycoside antibiotic neomycin and HIV Tat peptide-TAR RNA. © 1999 John Wiley & Sons, Inc. Med Res Rev, 19, No. 4, 307–319, 1999.
Databáze:	OpenAIRE
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