Abstract.
An electrospray ionization (ESI) ambient pressure ion-mobility spectrometer (APIMS) interfaced to an orthogonal reflector time-of-flight mass spectrometer (TOFMS) was evaluated for the first time as a detector for the identification of phenylthiohydantoin (PTH)-derivatized amino acids, the final products in the Edman sequencing process of peptides and proteins. The drift and flight times of the twenty common PTH amino acids were characterized by a well-defined 2-D mobility/mass spectral pattern. The combination of mobility/mass modes of analysis gave rise to a unique trend-line formation for the series of PTH amino acids. In addition, each PTH amino acid had a unique reduced mobility constant Ko, thus enabling the differentiation of all the amino acid derivatives including the PTH-leucine and PTH-isoleucine isomers. More importantly it was shown that it was possible to resolve a complete reference mixture of PTH amino acids in a single experimental run in less than 1 min. Detection limits for the PTH amino acids were found to range from 1.04 to 3.52 ng; indicating that the limits of detection were less than 17.0 pmol for all of the PTH amino acids.
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Steiner, W.E., Clowers, B.H. & Hill, H.H. Rapid separation of phenylthiohydantoin amino acids: ambient pressure ion-mobility mass spectrometry (IMMS). Anal Bioanal Chem 375, 99–102 (2003). https://doi.org/10.1007/s00216-002-1622-2
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DOI: https://doi.org/10.1007/s00216-002-1622-2