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

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

Journal Name: Protein & Peptide Letters

Volume 17 , Issue 2 , 2010

Become EABM
Become Reviewer

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.

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

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 17
ISSUE: 2
Year: 2010
Page: [168 - 171]
Pages: 4
DOI: 10.2174/092986610790225969
Price: $58

Article Metrics

PDF: 7