Analysis of synthetic peptides using matrix-assisted laser desorption ionization mass spectrometry.
Matrix-assisted laser desorption ionization mass spectroscopy (LDI MS), a novel method for analysis of large molecules, has been used for characterization of synthetic peptides and their by-products. The potential of LDI MS is demonstrated by analyzing crude synthetic peptides representing typical members of newly designed peptides and proteins. In the first case, a fragment condensation reaction yielding a highly hydrophobic six-helic bundle template-assembled synthetic protein (TASP) is monitored. Then, a crude 19-mer peptide designed to adopt an amphiphilic alpha-helical structure and its by-products from SPPS are identified. Finally, analysis of crude hirulog-1, a 20-mer peptide designed as a thrombin inhibitor, using C18 reversed phase high performance liquid chromatography (RP HPLC), capillary electrophoresis (CE) and LDI MS, manifests the potential of the latter method.
Steiner
V
V
Ciba-Geigy Ltd., Basel, Switzerland.
Börnsen
K O
KO
Schär
M
M
Gassmann
E
E
Hoffstetter-Kuhn
S
S
Rink
H
H
Mutter
M
M
D000595:Amino Acid Sequence; D007834:Lasers; D013058:Mass Spectrometry / Q000379:methods*; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D013917:Thrombin / Q000037:antagonists & inhibitors
D010455:Peptides; D013917:Thrombin