Stability comparison between sample preparation procedures for mass spectrometry-based targeted or shotgun peptidomic analysis

Beaudry, Francis

doi:10.1016/j.ab.2010.08.017

Cited by 10 publications

(3 citation statements)

References 19 publications

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“…However, natural hydrolysis of proteins can increase the complexity of data and is unfavorable for the study of endogenous peptides. Studies on humans and animals have shown that protease inhibitors alone are insufficient to prevent the degradation of endogenous peptides (Beaudry et al, 2010). Heating, such as through the use of a constant-temperature water bath, can effectively deactivate protein hydrolysis activity in samples by denaturing animal protein hydrolysis enzymes.…”

Section: Discussionmentioning

confidence: 99%

Identification of endogenous peptides in maize

Yin¹,

Li²,

Zhao³

et al. 2023

IJBLS

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The extraction and identification of endogenous peptides from plants are relatively unexplored because of the degradation of peptides after extraction from plant tissues. In this study, we developed an optimized sample preparation protocol that combined constant water heating with plant protease inhibitors and TCA-acetone precipitation, resulting in the effective extraction of endogenous peptide from plants, such as maize, while diminishing unspecific protease activity. The results showed that a total of 2867 endogenous peptides were identified in three maize samples using this method, of which 2119 (73.9%) peptides were commonly identified in all three samples. The length and molecular weight of these peptides ranged from 8 to 25 amino acids and from 729.44 to 2980.62 Da, respectively, with 96.4% of the peptide scores greater than 40. These results indicated that our extraction method is highly reproducible, precise, and wide-ranging, providing optimized information for large-scale identification of plant endogenous peptides.

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Section: Discussionmentioning

confidence: 99%

Identification of endogenous peptides in maize

Yin¹,

Li²,

Zhao³

et al. 2023

IJBLS

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“…As we described previously [Beaudry, 2010], tissue processing is an important step in preserving neuropeptides from in situ degradation. Mouse tissues were weighed accurately and homogenized using a tissue tearor following the addition of 0.25 % TFA solution at a ratio of 1:5 (w/v) resulting in a pH < 3.…”

Section: Sample Preparationmentioning

confidence: 99%

Liquid chromatography-electrospray linear ion trap mass spectrometry analysis of targeted neuropeptides in Tac1−/− mouse spinal cords reveals significant lower concentration of opioid peptides

Saidi

Beaudry

2015

Neuropeptides

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Tachykinin and opioid peptides play a central role in pain transmission, modulation and inhibition. The treatment of pain is very important in medicine and many studies using NK1 receptor antagonists failed to show significant analgesic effects in humans. Recent investigations suggest that both pronociceptive tachykinins and the analgesic opioid systems are important for normal pain sensation. The analysis of opioid peptides in Tac1 -/-spinal cord tissues offers a great opportunity to verify the influence of the tachykinin system on specific opioid peptides. The objectives of this study were to develop a HPLC-MS/MRM assay to quantify targeted peptides in spinal cord tissues. Secondly, we wanted to verify if the Tac1 -/-mouse endogenous opioid system is hampered and therefore affect significantly the pain modulatory pathways. Targeted neuropeptides were analyzed by high performance liquid chromatography linear ion trap mass spectrometry. Our results reveal that EM-2, Leu-Enk and Dyn A were down-regulated in Tac1 -/-spinal cord tissues. Interestingly, Dyn A was almost 3 fold down-regulated (p < 0.0001). No significant concentration differences were observed in mouse Tac1 -/-spinal cords for Met-Enk and CGRP. The analysis of Tac1 -/-mouse spinal cords revealed noteworthy decreases of EM-2, Leu-Enk and Dyn A concentrations which strongly suggest a significant impact on the endogenous pain-relieving mechanisms. These observations may have insightful impact on future analgesic drug developments and therapeutic strategies.3

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“…Peptidomic analysis has been proposed by several authors [43][44][45][46][47][48][49][50][51][52][53][54][55] as a way to access information relevant to clinical diagnosis and/or to monitor the patient biochemical profile during the therapy. The growing interest in peptidomic analysis led some scientists to develop new analytical technologies to improve peptidomic analysis, such as: use of capillary electrophoresis to separate the peptides [46]; use of size exclusion chromatography as a pre-fractionation step [53,56]; new technologies and methods for sample pretreatment [57], such as methods for isolation rare amino acid-containing peptides, terminal peptides, PTM peptides and endogenous peptides, automated sample pretreatment technologies (automated sample injection and on-line digestion) [58]; development of a new target plate for MALDI-MS for one step electric transfer of analytes from a 1-dimensional electrophoresis gel directly to the target plate [59,60]; etc. In recent years, in the face of the remarkable development on nanotechnology, many researchers have produced different kind of nanoparticles, such as mesoporous silica nanoparticles [50,51,61,62] and carbon nanotubes [52,63], for selective peptide extraction (and, hence, its enrichment) from biological fluids for therapeutic purposes (clinical diagnosis and/or novel biomarker discovery).…”

Section: Proteomic and Peptidomic Analysis: A New Approach To Study Vmentioning

confidence: 99%

Peptidomic Analysis of Animal Venoms

Cunha¹

2013

An Integrated View of the Molecular Recognition and Toxinology - From Analytical Procedures to Biomedical Applications

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Stability comparison between sample preparation procedures for mass spectrometry-based targeted or shotgun peptidomic analysis

Cited by 10 publications

References 19 publications

Identification of endogenous peptides in maize

Identification of endogenous peptides in maize

Liquid chromatography-electrospray linear ion trap mass spectrometry analysis of targeted neuropeptides in Tac1−/− mouse spinal cords reveals significant lower concentration of opioid peptides

Peptidomic Analysis of Animal Venoms

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