@ARTICLE{Cerrato2021,
author={Cerrato, A. and Aita, S.E. and Cavaliere, C. and Laganà, A. and Montone, C.M. and Piovesana, S. and Zenezini Chiozzi, R. and Capriotti, A.L.},
title={Comprehensive identification of native medium-sized and short bioactive peptides in sea bass muscle},
journal={Food Chemistry},
year={2021},
volume={343},
doi={10.1016/j.foodchem.2020.128443},
art_number={128443},
note={cited By 0},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85094806393&doi=10.1016%2fj.foodchem.2020.128443&partnerID=40&md5=18e830d704b9bc6ea02a8c7dfbe6c423},
abstract={Native peptides from sea bass muscle were analyzed by two different approaches: medium-sized peptides by peptidomics analysis, whereas short peptides by suspect screening analysis employing an inclusion list of exact m/z values of all possible amino acid combinations (from 2 up to 4). The method was also extended to common post-translational modifications potentially interesting in food analysis, as well as non-proteolytic aminoacyl derivatives, which are well-known taste-active building blocks in pseudo-peptides. The medium-sized peptides were identified by de novo and combination of de novo and spectra matching to a protein sequence database, with up to 4077 peptides (2725 modified) identified by database search and 2665 peptides (223 modified) identified by de novo only; 102 short peptide sequences were identified (with 12 modified ones), and most of them had multiple reported bioactivities. The method can be extended to any peptide mixture, either endogenous or by protein hydrolysis, from other food matrices. © 2020 Elsevier Ltd},
publisher={Elsevier Ltd},
issn={03088146},
coden={FOCHD},
pubmed_id={33129615},
document_type={Article},
source={Scopus},
}

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