Identification of bioactive short peptides in cow milk by high-performance liquid chromatography on C18 and porous graphitic carbon coupled to high-resolution mass spectrometry

Montone, Carmela Maria; Capriotti, Anna Laura; Cerrato, Andrea; Antonelli, Michela; Barbera, Giorgia La; Piovesana, Susy; Laganà, Aldo; Cavaliere, Chiara

doi:10.1007/s00216-019-01815-0

Cited by 34 publications

(22 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, already in 1992 synthetic di-peptides containing only Leu and Lys units were reported to be active against both Gram-negative and Gram-positive bacterial strains [ 47 ]; tri-peptides containing Leu, Lys and Trp residues have also been evaluated for antimicrobial activity after de novo identification [ 48 ]. In the BIOPEP database, 2 short AMPs are already presented and validated in milk samples [ 19 , 20 ]. Moreover, some recent studies have demonstrated that shorter peptides possess different advantages in preparation, less toxicity, and stability [ 49 ].…”

Section: Resultsmentioning

confidence: 99%

“…Samples were analyzed by RP chromatography as previously described [ 19 ] on a UHPLC Vanquish binary pump H coupled to a Q Exactive mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) by a heated electrospray (ESI) source. Samples were injected onto a Kinetex XB-C18 (100 × 2.1 mm, 2.6 μm particle size, Phenomenex, Torrance, CA, USA) operated at 40 °C.…”

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%

See 2 more Smart Citations

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

Cerrato

Capriotti

Capuano

et al. 2020

Foods

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

Cerrato

Capriotti

Capuano

et al. 2020

Foods

Self Cite

View full text Add to dashboard Cite

show abstract

“…The short peptides were analyzed by reverse-phase (RP) chromatography, using the Vanquish H UHPLC system coupled to an Q Exactive mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) and a heated electrospray source (ESI) [ 23 ]. The instrument was calibrated every 48 h using a Pierce LTQ Velos ESI Positive Ion Calibration Solution (Thermo Fisher Scientific); mass accuracy was <1 ppm.…”

Section: Methodsmentioning

confidence: 99%

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

et al. 2021

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…However, from a nutritional point of view, short-sized peptides (2-4 a.a.) are of more significant interest. Their short sequences allow them to be effectively absorbed intact from the gastrointestinal, preserving their structure [21,22]. As a result, it is presumable that short peptide sequences will not be subject to in vivo transformation that could affect their biological properties.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2021

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Identification of bioactive short peptides in cow milk by high-performance liquid chromatography on C18 and porous graphitic carbon coupled to high-resolution mass spectrometry

Cited by 34 publications

References 33 publications

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

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

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

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

Contact Info

Product

Resources

About