A new opening for the tricky untargeted investigation of natural and modified short peptides

Cerrato, Andrea; Aita, Sara Elsa; Capriotti, Anna Laura; Cavaliere, Chiara; Montone, Carmela Maria; Laganà, Aldo; Piovesana, Susy

doi:10.1016/j.talanta.2020.121262

Cited by 34 publications

(49 citation statements)

References 42 publications

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“…The identification of short peptides in fractionated gastrointestinal digests was performed following a data processing workflow implemented on Compound Discoverer (v. 3.1, Thermo Fisher Scientific, Bremen, Germany) [ 25 ]. The masses were extracted from the raw files based on customized parameters, aligning the signals, removing empty or missing MS/MS spectrum signals, and using short lists of complete peptides to match a possible composition.…”

Section: Methodsmentioning

confidence: 99%

Production and Characterization of Medium-Sized and Short Antioxidant Peptides from Soy Flour-Simulated Gastrointestinal Hydrolysate

et al. 2021

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Soybeans (Glycine max) are an excellent source of dietary proteins and peptides with potential biological activities, such as antihypertensive, anti-cholesterol, and antioxidant activity; moreover, they could prevent cancer. Also, soy contains all the essential amino acids for nutrition; therefore, it represents an alternative to animal proteins. The goal of this paper was the comprehensive characterization of medium-sized and short peptides (two to four amino acids) obtained from simulated gastrointestinal digestion. Two different analytical approaches were employed for peptide characterization, namely a common peptidomic analysis for medium-sized peptides and a suspect screening analysis for short peptides, employing an inclusion list of exact m/z values of all possible amino acid combinations. Moreover, fractionation by preparative reversed-phase liquid chromatography was employed to simplify the starting protein hydrolysate. Six fractions were collected and tested for antioxidative activity by an innovative antioxidant assay on human gastric adenocarcinoma AGS cell lines. The two most active fractions (2 and 3) were then characterized by a peptidomic approach and database search, as well as by a suspect screening approach, in order to identify potential antioxidant amino acid sequences. Some of the peptides identified in these two fractions have been already reported in the literature for their antioxidant activity.

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Section: Methodsmentioning

confidence: 99%

Production and Characterization of Medium-Sized and Short Antioxidant Peptides from Soy Flour-Simulated Gastrointestinal Hydrolysate

et al. 2021

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“…The identification of short peptides in the GCB extracts was accomplished as described thanks to a dedicated data processing workflow implemented on Compound Discoverer (v. 3.1, Thermo Fisher Scientific, Bremen, Germany) [ 22 ]. Briefly, the workflow allowed to extract the masses from the raw data files according to customized parameters for predicting the composition tool, aligning them, removing the signals of the blank or lacking MS/MS spectrum and using the comprehensive short peptide lists to match the extracted features.…”

Section: Methodsmentioning

confidence: 99%

“…Regarding small peptides (2–4 amino acids long), at present, only two studies reported the identification of two antimicrobial tripeptides (IQY and YVL) and two antimicrobial tetrapeptides (EIPT and CIRA) generated by the enzymatic hydrolysis of bovine lactoferrin and kappa casein. The small number of publications on short AMPs is mainly ascribed to the several issues in the separation and identification of small amino acidic sequences [ 19 , 20 , 21 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and Antimicrobial Activity of Medium-Sized and Short Peptides from Yellowfin Tuna (Thunnus albacares) Simulated Gastrointestinal Digestion

Cerrato

Capriotti

Capuano

et al. 2020

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Due to the rapidly increasing resistance to conventional antibiotics, antimicrobial peptides are emerging as promising novel drug candidates. In this study, peptide fragments were obtained from yellowfin tuna muscle by simulated gastrointestinal digestion, and their antimicrobial activity towards Gram-positive and Gram-negative bacteria was investigated. In particular, the antimicrobial activity of both medium- and short-sized peptides was investigated by using two dedicated approaches. Medium-sized peptides were purified by solid phase extraction on C18, while short peptides were purified thanks to a graphitized carbon black sorbent. For medium-sized peptide characterization, a peptidomic strategy based on shotgun proteomics analysis was employed, and identification was achieved by matching protein sequence database by homology, as yellowfin tuna is a non-model organism, leading to the identification of 403 peptides. As for short peptide sequences, an untargeted suspect screening approach was carried out by means of an inclusion list presenting the exact mass to charge ratios (m/z) values for all di-, tri- and tetrapeptides. In total, 572 short sequences were identified thanks to a customized workflow dedicated to short peptide analysis implemented on Compound Discoverer software.

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“…Their small dimensions, in fact, hinder the generation of multi-charged adducts, and singly charged ions are much more likely to be generated. Moreover, the physicochemical properties of short peptide sequences are more dependent on the nature of the a.a., reflecting in more significant variability of the fragmentation pathways and resulting in the need for manual validation for proper identification [24]. Finally, database search, which associates amino acid sequences to existing peptides present in databases, cannot be employed with satisfying results for very short sequences.…”

Section: Hrms Data Acquisition and Short Peptide Identificationmentioning

confidence: 99%

High-Resolution Mass Spectrometry and Chemometrics for the Detailed Characterization of Short Endogenous Peptides in Milk By-Products

et al. 2021

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The process of cheese-making has long been part of human food culture and nowadays dairy represents a large sector of the food industry. Being the main byproduct of cheese-making, the revalorization of milk whey is nowadays one of the primary goals in alignment with the principles of the circular economy. In the present paper, a deep and detailed investigation of short endogenous peptides in milk and its byproducts (whole whey, skimmed whey, and whey permeate) was carried out by high-resolution mass spectrometry, with a dedicated suspect screening data acquisition and data analysis approach. A total of 79 short peptides was tentatively identified, including several sequences already known for their exerted biological activities. An unsupervised chemometric approach was then employed for highlighting the differences in the short peptide content among the four sets of samples. Whole and skimmed whey showed not merely a higher content of short bioactive peptides compared to whole milk, but also a peculiar composition of peptides that are likely generated during the process of cheese-making. The results clearly demonstrate that whey represents a valuable source of bioactive compounds and that the set-up of processes of revalorization of milk byproducts is a promising path in the obtention of high revenue-generating products from dairy industrial waste.

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A new opening for the tricky untargeted investigation of natural and modified short peptides

Cited by 34 publications

References 42 publications

Production and Characterization of Medium-Sized and Short Antioxidant Peptides from Soy Flour-Simulated Gastrointestinal Hydrolysate

Production and Characterization of Medium-Sized and Short Antioxidant Peptides from Soy Flour-Simulated Gastrointestinal Hydrolysate

Identification and Antimicrobial Activity of Medium-Sized and Short Peptides from Yellowfin Tuna (Thunnus albacares) Simulated Gastrointestinal Digestion

High-Resolution Mass Spectrometry and Chemometrics for the Detailed Characterization of Short Endogenous Peptides in Milk By-Products

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