Characterization of Chemical Modification of Tryptophan by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

Title: Characterization of Chemical Modification of Tryptophan by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

Volume: 17 Issue: 2

Author(s): C. Sivakama Sundari, K. Chakraborty, R. Nagaraj and M. V. Jagannadham

Affiliation:

Keywords: Tryptophan modification, peptide sequence, MALDI TOF/TOF, posttranslational modifications, acetylation

Abstract: Tert- butylation of tryptophan (2, 5, 7- tri tertiary butyl tryptophan), formed during acidolytic cleavage of synthetic peptides Ac-KLVYWAE-CONH2 (A-YW) and Ac-KLVWWAE-CONH2 (A-WW), that are analogs of the fragment of Alzheimers β-amyloid peptide Ac-KLVFFAE-CONH2, during solid-phase peptide synthesis, was characterized by matrix- assisted laser desorption/ionization time of flight/time of flight (MALDI TOF/TOF) mass spectrometry. Crude peptide was fractionated by high performance liquid chromatography. Peptide fractions were sequenced and modified tryptophan was determined with the help of MALDI TOF/TOF mass spectra. Thus, it is possible to pinpoint the particular tryptophan residue that undergoes modification during synthesis of peptides containing multiple tryptophan residues.

Cite this article as:

Sundari Sivakama C., Chakraborty K., Nagaraj R. and Jagannadham V. M., Characterization of Chemical Modification of Tryptophan by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry, Protein & Peptide Letters 2010; 17 (2) . https://dx.doi.org/10.2174/092986610790225969