The application of atmospheric pressure matrix-assisted laser desorption/ionization to the analysis of long-term cryopreserved serum peptidome |
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Authors: | Mangerini Rosa Romano Paolo Facchiano Angelo Damonte Gianluca Muselli Marco Rocco Mattia Boccardo Francesco Profumo Aldo |
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Affiliation: | aS.C. Oncologia Medica B, Istituto Nazionale per la Ricerca sul Cancro, 16132 Genova, Italy;bS.C. Anatomia e Citoistologia Patologica, Istituto Nazionale per la Ricerca sul Cancro, 16132 Genova, Italy;cIstituto di Scienze dell’Alimentazione, Consiglio Nazionale delle Ricerche, 83100 Avellino, Italy;dDipartimento di Medicina Sperimentale e Centro di Eccellenza per la Ricerca Biomedica, Università di Genova, 16132 Genova, Italy;eIstituto di Elettronica e di Ingegneria dell’Informazione e delle Telecomunicazioni, Consiglio Nazionale delle Ricerche, 16149 Genova, Italy;fS.S. Biopolimeri e Proteomica, Istituto Nazionale per la Ricerca sul Cancro, 16132 Genova, Italy;gDipartimento di Oncologia, Biologia e Genetica, Università di Genova, 16132 Genova, Italy |
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Abstract: | Although most time-of-flight (TOF) mass spectrometers come equipped with vacuum matrix-assisted laser desorption/ionization (MALDI) sources, the atmospheric pressure MALDI (API–MALDI) source is an attractive option because of its ability to be coupled to a wide range of analyzers. This article describes the use of an API–MALDI source coupled to a TOF mass spectrometer for evaluation of the effects of medium- and long-term storage on peptidomic profiles of cryopreserved serum samples from healthy women. Peptides were purified using superparamagnetic beads either from fresh sera or after serum storage at −80 °C for 18 months or at −20 °C for 8 years. Data were preprocessed using newly developed bioinformatic tools and then were subjected to statistical analysis and class prediction. The analyses showed a dramatic effect of storage on the abundance of several peptides such as fibrinopeptides A and B, complement fractions, bradykinin, and clusterin, indicated by other authors as disease biomarkers. Most of these results were confirmed by shadow clustering analysis, able to classify each sample in the correct group. In addition to demonstrating the suitability of the API–MALDI technique for peptidome profiling studies, our data are of relevance for retrospective studies that involve frozen sera stored for many years in biobanks. |
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Keywords: | Atmospheric pressure ionization MALDI&ndash TOF Peptidome profile Protein degradation Serum cryopreservation |
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