Teaching venturi electrospray mass spectrometry with amino acid analysis

Ribeiro, Matheus Henrique Dal Molin; Tonin, Angélica Priscila Parussolo; Poliseli, Camila B.; Lima, Beatriz Betone De; Castro, Luiz Eduardo Nochi; Silva, Valquíria M.; Valério, Marcelo; Cedran, Jaime C.; Meurer, Eduardo C.

doi:10.1016/j.ijms.2019.116183

Cited by 3 publications

(4 citation statements)

References 28 publications

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“…The acidic nature of the peptides likely made them soluble, forming ammonium salts: prior to analyses, these were diluted into the mobile phase with 0.1% of formic acid to protonate the molecules, forming NH 3 , CO 2 , and H 2 O. A mixture of four natural amino acids 14 was used to tune the mass spectrometer and to facilitate their proper detection using a NL of 46 Da. This procedure was carried out to achieve a better ionization performance for both di‐ and tripeptides.…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, our study aims to develop a fast LC–MS/MS method based on the neutral loss (NL) of 46 Da, in order to identify dipeptides and tripeptides candidates directly from protein hydrolysates, without the need of any laborious pre‐treatment or time‐consuming chromatographic separation. Protonated molecules of di‐ and tripeptides should be easily screened from their selective neutral loss (NL) of 46 Da loss due to the carboxylic acid moiety 14 and could also be screened from their collision‐induced dissociation (CID) fragments by de novo sequencing 15 . NL is a structural selective scaning mode that allows selective identification of organic ions 16 .…”

Section: Introductionmentioning

confidence: 99%

“…NL has been used, for instance, to analyze pooled samples to identify biomarkers in coronary arterial disease diagnosis and amorfrutin derivatives identification in real samples 17 . NL of 46 Da (CO and H 2 O or formic acid) comes from the carboxylic moiety of peptides 14 . Our study focused on a new method of di‐ and tripeptide analyses using important sources of peptides, as previously mentioned.…”

Section: Introductionmentioning

confidence: 99%

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Tri‐ and dipeptides identification in whey protein and porcine liver protein hydrolysates by fast LC–MS/MS neutral loss screening and de novo sequencing

et al. 2021

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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.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Tri‐ and dipeptides identification in whey protein and porcine liver protein hydrolysates by fast LC–MS/MS neutral loss screening and de novo sequencing

et al. 2021

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“…Ribeiro et al have described interesting experiments on the use of a venturi ESI source to analyse the amino acid mixtures. 36 In the venturi ESI source, a high velocity nebulization gas flows coaxially in a tube with an electrospray capillary tube inside. It results in the reduction in the pressure of the gas in the tube causing a self-pumping effect, thus the analysed solution is sucked to an ESI source, without a delivery system.…”

Section: Foundations Of Mass Spectrometrymentioning

confidence: 99%

Teaching mass spectrometry: A compilation of approaches to teaching theory and practice of mass spectrometry

Frański

2024

Eur J Mass Spectrom (Chichester)

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The areas of mass spectrometry applications seem to be much larger than those of any other analytical techniques. They extend from the determination of molecular mass in organic chemistry, through the analytical applications in forensic, environmental and omics sciences, the application in extra-terrestrial exploration and many others. Mass spectrometry, usually coupled with chromatographic techniques, has also found wide application in the pharmaceutical industry, forensic laboratories, laboratories of sanitary inspection or environmental inspection, etc. The growing areas of applications give rise to the demand for the comprehensive mass spectrometry education of undergraduates. This overview covers the body of literature describing various interesting ideas that can be successfully used for teaching mass spectrometry. Since mass spectrometry is a multidisciplinary field, old but dynamically developing, teaching mass spectrometry may be more problematic in comparison to teaching other analytical techniques, for example, there is the problem of position of mass spectrometry in the chemistry curriculum. On the other hand, it is obvious that the mass spectrometry community, besides difficult scientific work, does great and admirable teaching work, in order to perfectly educate undergraduates in the field of mass spectrometry and to make learning mass spectrometry as attractive as possible.

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Cutting-edge developments in mass spectrometry: A hands-on workshop

Morato

Cooks

2020

International Journal of Mass Spectrometry

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Teaching venturi electrospray mass spectrometry with amino acid analysis

Cited by 3 publications

References 28 publications

Tri‐ and dipeptides identification in whey protein and porcine liver protein hydrolysates by fast LC–MS/MS neutral loss screening and de novo sequencing

Tri‐ and dipeptides identification in whey protein and porcine liver protein hydrolysates by fast LC–MS/MS neutral loss screening and de novo sequencing

Teaching mass spectrometry: A compilation of approaches to teaching theory and practice of mass spectrometry

Cutting-edge developments in mass spectrometry: A hands-on workshop

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