Identification of protein binders in artworks by MALDI-TOF/TOF tandem mass spectrometry
Само за регистроване кориснике
2013
Аутори
Tripković, T.Charvy, C.
Alves, S.
Lolić, Aleksandar
Baošić, Rada
Nikolić-Mandić, Snežana D.
Tabet, J. C.
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Aim of this work is to propose an analytical protocol for proteinaceous binder identification in paintings using tryptic peptide analysis and MALDI-TOF mass spectrometry strengthened with MALDI-TOF/TOF tandem mass spectrometry (LIFT method). Proteinaceous binders are enzymatically digested with trypsin. From each individual protein frequently occurring in binders, a specific set of peptides is releasing during enzymatic digestion giving a peptide mass fingerprint (PMF) of that particular protein. The most intensive peptide peaks in PMF were determined and annotated with their corresponding amino acid sequence by MALDI-TOF/TOF analysis and subsequent database search. Before analyzing historical painting samples, procedure was tested and optimized on several painting model samples for a reliable and efficient identification of proteinaceous materials. The method is avoiding sample manipulation as much as possible in order to reduce sample loss. Since the applied procedures led to protein... identification of binding media in model samples, MALDI-TOF/TOF was for the first time applied for analysis of proteinaceous binders in old painting samples.
Кључне речи:
MALDI TOF MS / LIFT-TOF/TOF tandem mass spectrometry / Peptide mass fingerprint / Proteinaceous binders / Historical paintingsИзвор:
Talanta, 2013, 113, 49-61Издавач:
- Elsevier Science Bv, Amsterdam
Финансирање / пројекти:
- Развој нових и побољшање постојећих електрохемијских, спектроскопских и проточних (FIA) метода за праћење квалитета животне средине (RS-MESTD-Basic Research (BR or ON)-172051)
Напомена:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3500
DOI: 10.1016/j.talanta.2013.03.071
ISSN: 0039-9140
PubMed: 23708623
WoS: 000320416500009
Scopus: 2-s2.0-84876786177
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Tripković, T. AU - Charvy, C. AU - Alves, S. AU - Lolić, Aleksandar AU - Baošić, Rada AU - Nikolić-Mandić, Snežana D. AU - Tabet, J. C. PY - 2013 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1366 AB - Aim of this work is to propose an analytical protocol for proteinaceous binder identification in paintings using tryptic peptide analysis and MALDI-TOF mass spectrometry strengthened with MALDI-TOF/TOF tandem mass spectrometry (LIFT method). Proteinaceous binders are enzymatically digested with trypsin. From each individual protein frequently occurring in binders, a specific set of peptides is releasing during enzymatic digestion giving a peptide mass fingerprint (PMF) of that particular protein. The most intensive peptide peaks in PMF were determined and annotated with their corresponding amino acid sequence by MALDI-TOF/TOF analysis and subsequent database search. Before analyzing historical painting samples, procedure was tested and optimized on several painting model samples for a reliable and efficient identification of proteinaceous materials. The method is avoiding sample manipulation as much as possible in order to reduce sample loss. Since the applied procedures led to protein identification of binding media in model samples, MALDI-TOF/TOF was for the first time applied for analysis of proteinaceous binders in old painting samples. PB - Elsevier Science Bv, Amsterdam T2 - Talanta T1 - Identification of protein binders in artworks by MALDI-TOF/TOF tandem mass spectrometry VL - 113 SP - 49 EP - 61 DO - 10.1016/j.talanta.2013.03.071 ER -
@article{ author = "Tripković, T. and Charvy, C. and Alves, S. and Lolić, Aleksandar and Baošić, Rada and Nikolić-Mandić, Snežana D. and Tabet, J. C.", year = "2013", abstract = "Aim of this work is to propose an analytical protocol for proteinaceous binder identification in paintings using tryptic peptide analysis and MALDI-TOF mass spectrometry strengthened with MALDI-TOF/TOF tandem mass spectrometry (LIFT method). Proteinaceous binders are enzymatically digested with trypsin. From each individual protein frequently occurring in binders, a specific set of peptides is releasing during enzymatic digestion giving a peptide mass fingerprint (PMF) of that particular protein. The most intensive peptide peaks in PMF were determined and annotated with their corresponding amino acid sequence by MALDI-TOF/TOF analysis and subsequent database search. Before analyzing historical painting samples, procedure was tested and optimized on several painting model samples for a reliable and efficient identification of proteinaceous materials. The method is avoiding sample manipulation as much as possible in order to reduce sample loss. Since the applied procedures led to protein identification of binding media in model samples, MALDI-TOF/TOF was for the first time applied for analysis of proteinaceous binders in old painting samples.", publisher = "Elsevier Science Bv, Amsterdam", journal = "Talanta", title = "Identification of protein binders in artworks by MALDI-TOF/TOF tandem mass spectrometry", volume = "113", pages = "49-61", doi = "10.1016/j.talanta.2013.03.071" }
Tripković, T., Charvy, C., Alves, S., Lolić, A., Baošić, R., Nikolić-Mandić, S. D.,& Tabet, J. C.. (2013). Identification of protein binders in artworks by MALDI-TOF/TOF tandem mass spectrometry. in Talanta Elsevier Science Bv, Amsterdam., 113, 49-61. https://doi.org/10.1016/j.talanta.2013.03.071
Tripković T, Charvy C, Alves S, Lolić A, Baošić R, Nikolić-Mandić SD, Tabet JC. Identification of protein binders in artworks by MALDI-TOF/TOF tandem mass spectrometry. in Talanta. 2013;113:49-61. doi:10.1016/j.talanta.2013.03.071 .
Tripković, T., Charvy, C., Alves, S., Lolić, Aleksandar, Baošić, Rada, Nikolić-Mandić, Snežana D., Tabet, J. C., "Identification of protein binders in artworks by MALDI-TOF/TOF tandem mass spectrometry" in Talanta, 113 (2013):49-61, https://doi.org/10.1016/j.talanta.2013.03.071 . .