Premium
Application of mass spectrometry for target identification and characterization
Author(s) -
Loo Joseph A.,
DeJohn Dana E.,
Du Ping,
Stevenson Tracy I.,
Ogorzalek Loo Rachel R.
Publication year - 1999
Publication title -
medicinal research reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.868
H-Index - 130
eISSN - 1098-1128
pISSN - 0198-6325
DOI - 10.1002/(sici)1098-1128(199907)19:4<307::aid-med4>3.0.co;2-2
Subject(s) - mass spectrometry , identification (biology) , chemistry , characterization (materials science) , computational biology , chromatography , biology , nanotechnology , materials science , botany
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.