Example：10.1021/acsami.1c06204 or Chem. Rev., 2007, 107, 2411-2502
Tri‐ and dipeptides identification in whey protein and porcine liver protein hydrolysates by fast LC–MS/MS neutral loss screening and de novo sequencing Journal of Mass Spectrometry (IF1.982), Pub Date : 2020-12-29, DOI: 10.1002/jms.4701 Camila B. Poliseli, Angelica P.P. Tonin, Fernanda C. Martinez, Nicholas C. do Nascimento, Vilmar Braz, Jose Maluf, Valquiria M.S. Ribeiro, Fernanda A. Della Rosa, Gustavo H.M.F. Souza, Eduardo C. Meurer
We describe a fast (5 min) liquid chromatography tandem mass spectrometry method (LC–MS/MS) based on a 46 Da neutral loss of formic acid (H2O and CO) to identify tri‐ and dipeptides (DIPEP) in whey protein and porcine liver protein hydrolysates and confirmed by further de novo sequencing. Sample solutions were acidified to favor [dipep + H]+ ions, and a m/z range of 50–300 was used to improve sensitivity. All dipeptide candidates were selected based on all possibilities of the 20 amino acid combinations, and their collision‐induced dissociation fragments were screened via de novo sequencing. To determine their biological activities, sequenced dipeptides were compared with the Biopep database and other data from literature. Altogether, 18 dipeptides and 7 tripeptides were identified from the whey protein hydrolysate; they seemed to be broadly active, and peptides were identified as active dipeptidyl peptidase IV inhibitors and active angiotensin‐converting enzyme (ACE), according to available information. Porcine liver hydrolysate showed 14 dipeptides which exhibit similar biological activities to whey protein hydrolysate.