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Comparison between enhanced MALDI in-source decay by ammonium persulfate and N- or C-terminal derivatization methods for detailed peptide structure determination


Horvatić, Anita; Dodig, Ivana; Vuletić, Tomislav; Pavoković, Dubravko; Hameršak, Zdenko; Butorac, Ana; Cindrić, Mario
Comparison between enhanced MALDI in-source decay by ammonium persulfate and N- or C-terminal derivatization methods for detailed peptide structure determination // Analytical chemistry, 85 (2013), 8; 3940-3947 doi:10.1021/ac303436n (međunarodna recenzija, članak, znanstveni)


Naslov
Comparison between enhanced MALDI in-source decay by ammonium persulfate and N- or C-terminal derivatization methods for detailed peptide structure determination

Autori
Horvatić, Anita ; Dodig, Ivana ; Vuletić, Tomislav ; Pavoković, Dubravko ; Hameršak, Zdenko ; Butorac, Ana ; Cindrić, Mario

Izvornik
Analytical chemistry (0003-2700) 85 (2013), 8; 3940-3947

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
MALDI-TOF/TOF; mobile and localized proton; enhanced pseudo-MS; SPITC-4-sulfophenyl-isothiocyanate; Lys-tag-2-methoxy-4; 5-dihydro-1H-imidazole; ammonium persulfate (APS)

Sažetak
Amino acid sequencing and more detailed structure elucidation analysis of peptides and small proteins is a very difficult task even if state-of-the-art mass spectrometry (MS) is employed. To make this task easier, chemical derivatization methods of the N terminus with 4-sulfophenyl-isothiocyanate (SPITC) or the C terminus with 2-methoxy-4, 5-dihydro-1H-imidazole (Lys-tag) can enhance peptide fragmentation or fragment ionizability, via proton mobility/localization mechanisms making tandem MS (MS2) spectra more informative and less demanding for structural interpretation. Observed disadvantages related to both derivatization methods are sample- and time-consuming procedures and the increased number of reaction byproducts. A novel, sulfate radical in-source formation method of matrix-assisted laser desorption ionization (MALDI) MS based on chemically enhanced in-source decay (ISD) can be accomplished by simple addition of ammonium persulfate (APS) in the matrix solution. This method enables effective decomposition of peptide ions already in the first stage of MS analysis where a large number of fragment ions are produced. The resultant MALDI-ISD mass spectra (MS after APS → MALDI-ISD MS) are almost equivalent to conventional, collision-induced dissociation (CID) MS2 spectra. These fragment ions are further subjected to the second stage of the MS, and consequently, MS3 spectra are produced, which makes the sequence analysis more informative and complete (CID MS2 is thus equivalent to CID MS3). Multiply stage MS after APS addition showed enhanced sensitivity, resolution, and mass accuracy compared to peptide derivatization (SPITC and Lys-tag) or conventional MS and MS2 analyses and offered more detailed insight into peptide structure.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekt / tema
098-0000000-3454 - Proteomska analiza tkiva u bolesnika s karcinomom prostate (Mario Cindrić, )

Ustanove
Institut za fiziku, Zagreb,
Prehrambeno-biotehnološki fakultet, Zagreb,
Institut "Ruđer Bošković", Zagreb,
Prirodoslovno-matematički fakultet, Zagreb,
Fakultet kemijskog inženjerstva i tehnologije, Zagreb

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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