![]() ![]() De novo peptide sequencing and identification with precision mass spectrometry. 2011 10:M110.003822.įrank AM, Savitski MM, Nielsen ML, Zubarev RA, Pevzner PA. Hierarchical clustering of shotgun proteomics data. Koskinen VR, Emery PA, Creasy DM, Cottrell JS. Peptidome characterization and bioactivity analysis of donkey milk. Piovesana S, Capriotti AL, Cavaliere C, La Barbera G, Samperi R, Zenezini Chiozzi R, et al. Purification and identification of endogenous antioxidant and ACE-inhibitory peptides from donkey milk by multidimensional liquid chromatography and nanoHPLC-high resolution mass spectrometry. Zenezini Chiozzi R, Capriotti AL, Cavaliere C, La Barbera G, Piovesana S, Samperi R, et al. Comprehensive peptidomic and glycomic evaluation reveals that sweet whey permeate from colostrum is a source of milk protein-derived peptides and oligosaccharides. 2013 61:9110–7.ĭallas DC, Weinborn V, de Moura Bell JMLN, Wang M, Parker EA, Guerrero A, et al. Identification of multiphosphorylated peptides in milk. Analysis of the endogenous peptide profile of milk: identification of 248 mainly casein-derived peptides. 2017 221:1895–903.īaum F, Fedorova M, Ebner J, Hoffmann R, Pischetsrieder M. Comparative analysis of human milk and infant formula derived peptides following in vitro digestion. Su M-Y, Broadhurst M, Liu C-P, Gathercole J, Cheng W-L, Qi X-Y, et al. Human milk peptides differentiate between the preterm and term infant and across varying lactational stages. 2019 274:766–74.ĭingess KA, de Waard M, Boeren S, Vervoort J, Lambers TT, van Goudoever JB, et al. Peptidomic profiling of human milk with LC–MS/MS reveals pH-specific proteolysis of milk proteins. Gan J, Robinson RC, Wang J, Krishnakumar N, Manning CJ, Lor Y, et al. Recent trends in the analysis of bioactive peptides in milk and dairy products. 2015 35:831–40.Ĭapriotti AL, Cavaliere C, Piovesana S, Samperi R, Laganà A. Bioactive peptides in milk and dairy products: a review. ![]() The method allowed the untargeted identification of short peptides in milk, a complex matrix chosen as a representative real sample for method application, and provides complementary information to that accessible by ordinary peptidomics. The results indicated that an integrated approach may be appropriate to improve the separation of different peptides and increase the number of identifications because of the wide range of polarity of short peptides. A total of 57 and 41 peptides were identified by using a C18 and a PGC column, respectively in particular, 31 were exclusively identified by using the C18 column, 15 unique peptides were identified by using the PGC column, while 26 were in common between the two data sets, demonstrating that the two columns have a different selectivity mechanism. By this approach, the method allowed the separation and characterization of di-, tri- and tetrapeptides. The sample was then separated by means of two chromatographic columns, with a complementary selectivity mechanism, namely reversed-phase C18 column and porous graphitic carbon (PGC). After milk defatting and precipitation, the sample was purified by cotton-hydrophilic interaction liquid chromatography (HILIC) micro tip in order to avoid suppression phenomena due to contaminants present in milk, such as carbohydrates. In particular, in this work an untargeted peptidomic approach based on ultrahigh-performance liquid chromatography coupled to high-resolution mass spectrometry was developed for the identification of short peptides in cow milk samples. ![]() The method described in this paper comprises a combination of strategies to tackle the main limitations in short peptide analysis. Despite the importance of short peptides, they are currently less studied than other peptides because of the lack of dedicated methods for their characterization. Short peptides are important compounds in a variety of fields, including food and nutraceutical applications, but also biomarker discovery, bioactive peptide discovery and peptide drug separation. ![]()
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