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Clustering analyses in peptidomics revealed that peptide profiles of infant formulae are descriptive.

ABSTRACT: Prompted by the accumulating evidence on bioactive moieties of milk-derived peptides, novel methods were applied to compare the peptide composition among commercially available hydrolysate formulations and to determine batch-to-batch variations of protein hydrolysate products. Despite the availability of general methods to measure, for example, the degree of hydrolysis and peptide mass distribution at a high level, the objective of this study was to more qualitatively compare peptide sequences and composition. By a comprehensive approach combining peptidomics technologies and multivariate clustering analyses, the peptide profiles of different hydrolyzed milk protein formulations were compared. Moreover, peptide profiles of various hydrolysate batches that had been produced over a period of 5 years were included. Coupling of identified peptide sequences to the position in their corresponding milk proteins produced numerical datasets that subsequently were utilized for multivariate data analyses. These analyses revealed that batch-to-batch variation in the peptide profiles of a specific extensively hydrolyzed casein preparation was low. Moreover, extensive multivariate evaluations revealed that the peptide profiles of different commercially available hydrolyzed milk protein formulations provided a descriptive and distinct signature. Overall, the described methodology may contribute to the field of peptide research as observed dissimilarities in peptide profiles of similar products may be related to differences in their overall functionality.

SUBMITTER: Lambers TT

PROVIDER: S-EPMC4304566 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature

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Clustering analyses in peptidomics revealed that peptide profiles of infant formulae are descriptive.

Lambers Tim T TT Gloerich Jolein J van Hoffen Els E Alkema Wynand W Hondmann Dirk H DH van Tol Eric Af EA

Food science & nutrition 20141230 1

Prompted by the accumulating evidence on bioactive moieties of milk-derived peptides, novel methods were applied to compare the peptide composition among commercially available hydrolysate formulations and to determine batch-to-batch variations of protein hydrolysate products. Despite the availability of general methods to measure, for example, the degree of hydrolysis and peptide mass distribution at a high level, the objective of this study was to more qualitatively compare peptide sequences a ...[more]

PMID: 25648153

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Project description:Analysis of native or endogenous peptides in biofluids can provide valuable insights into disease mechanisms. Furthermore, the detected peptides may also have utility as potential biomarkers for non-invasive monitoring of human diseases. The non-invasive nature of urine collection and the abundance of peptides in the urine makes analysis by high-throughput 'peptidomics' methods , an attractive approach for investigating the pathogenesis of renal disease. However, urine peptidomics methodologies can be problematic with regards to difficulties associated with sample preparation. The urine matrix can provide significant background interference in making the analytical measurements that it hampers both the identification of peptides and the depth of the peptidomics read when utilizing LC-MS based peptidome analysis. We report on a novel adaptation of the standard solid phase extraction (SPE) method to a modified SPE (mSPE) approach for improved peptide yield and analysis sensitivity with LC-MS based peptidomics in terms of time, cost, clogging of the LC-MS column, peptide yield, peptide quality, and number of peptides identified by each method. Expense and time requirements were comparable for both SPE and mSPE, but more interfering contaminants from the urine matrix were evident in the SPE preparations (e.g., clogging of the LC-MS columns, yellowish background coloration of prepared samples due to retained urobilin, lower peptide yields) when compared to the mSPE method. When we compared data from technical replicates of 4 runs, the mSPE method provided significantly improved efficiencies for the preparation of samples from urine (e.g., mSPE peptide identification 82% versus 18% with SPE; p = 8.92E-05). Additionally, peptide identifications, when applying the mSPE method, highlighted the biology of differential activation of urine peptidases during acute renal transplant rejection with distinct laddering of specific peptides, which was obscured for most proteins when utilizing the conventional SPE method. In conclusion, the mSPE method was found to be superior to the conventional, standard SPE method for urine peptide sample preparation when applying LC-MS peptidomics analysis due to the optimized sample clean up that provided improved experimental inference from the confidently identified peptides.

Project description:Post-natal gut maturation in infants interrelates maturation of the morphology, digestive, and immunological functions and gut microbiota development. Here, we explored both microbiota development and markers of gut barrier and maturation in healthy term infants during their early life to assess the interconnection of gut functions during different infant formulae regimes. A total of 203 infants were enrolled in this randomized double-blind controlled trial including a breastfed reference group. Infants were fed starter formulae for the first four weeks of life, supplemented with different combination of nutrients (lactoferrin, probiotics (Bifidobacterium animal subsp. Lactis) and prebiotics (Bovine Milk-derived Oligosaccharides-BMOS)) and subsequently fed the control formula up to eight weeks of life. Stool microbiota profiles and biomarkers of early gut maturation, calprotectin (primary outcome), elastase, α-1 antitrypsin (AAT) and neopterin were measured in feces at one, two, four, and eight weeks. Infants fed formula containing BMOS had lower mean calprotectin levels over the first two to four weeks compared to the other formula groups. Elastase and AAT levels were closer to levels observed in breastfed infants. No differences were observed for neopterin. Global differences between the bacterial communities of all groups were assessed by constrained multivariate analysis with hypothesis testing. The canonical correspondence analysis (CCA) at genus level showed overlap between microbiota profiles at one and four weeks of age in the BMOS supplemented formula group with the breastfed reference, dominated by bifidobacteria. Microbiota profiles of all groups at four weeks were significantly associated with the calprotectin levels at 4 (CCA, p = 0.018) and eight weeks of age (CCA, p = 0.026). A meaningful correlation was observed between changes in microbiota composition and gut maturation marker calprotectin. The supplementation with BMOS seems to favor gut maturation closer to that of breastfed infants.

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Clustering analyses in peptidomics revealed that peptide profiles of infant formulae are descriptive.

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Clustering analyses in peptidomics revealed that peptide profiles of infant formulae are descriptive.

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