Developing mass spectrometry for the quantitative analysis of neuropeptides

Phetsanthad, Ashley; Riusech, Olga L

doi:10.1080/14789450.2021.1967146

Cited by 10 publications

(6 citation statements)

References 170 publications

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“…Second, this modus operandi severely impacts reproducibility, since peak selection in DDA is stochastic, with different peaks being selected even when the identical sample is measured several times. The demand for LC–MS/MS strategies overcoming the low sensitivity and low reproducibility of DDA as well as enabling robust quantification of neuropeptides has been voiced recently ( 75 ). PRM itself has already been used previously for this purpose but was mostly limited to target a handful of neuropeptides ( 63 ), in contrast to the several hundred described in this study.…”

Section: Discussionmentioning

confidence: 99%

Mass Spectrometry–Driven Discovery of Neuropeptides Mediating Nictation Behavior of Nematodes

Cockx

Bael

Boelen

et al. 2023

Molecular & Cellular Proteomics

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Section: Discussionmentioning

confidence: 99%

Mass Spectrometry–Driven Discovery of Neuropeptides Mediating Nictation Behavior of Nematodes

Cockx

Bael

Boelen

et al. 2023

Molecular & Cellular Proteomics

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“…While its fundamental working principle aligns with vacuum MALDI, AP‐MALDI mitigates sample dehydration and vacuum‐induced sample changes, leading to enhanced operational convenience 11,12 . During AP‐MALDI MS tissue imaging studies, special care should be taken with sample preparation to decrease the effect of ion suppression limiting peptide ion yield 13 …”

Section: Introductionmentioning

confidence: 99%

“…11,12 During AP-MALDI MS tissue imaging studies, special care should be taken with sample preparation to decrease the effect of ion suppression limiting peptide ion yield. 13 Peptides in AP-MALDI MS tissue imaging studies can be made more visible by improving conditions for better co-crystallization between target analytes and matrix material. Also, removal of salts and high-abundance species, such as lipids, causing the ion suppression effect, significantly improves the peptide ion yield.…”

mentioning

confidence: 99%

Imaging and quantification of neuropeptides in mouse pituitary tissue by atmospheric pressure matrix‐assisted laser desorption/ionization mass spectrometry

Yang,

Liu,

et al. 2024

Rapid Comm Mass Spectrometry

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RationaleAtmospheric pressure matrix‐assisted laser desorption/ionization (AP‐MALDI) mass spectrometry has enabled the untargeted analysis and imaging of neuropeptides and proteins in biological tissues under ambient conditions. Sensitivity in AP‐MALDI can be improved by using sample‐specific preparation methods.MethodsA comprehensive and detailed optimization strategy including instrument parameters, matrix spraying and sample tissue washing pretreatment was implemented to enhance the sensitivity and coverage of neuropeptides in mouse pituitary tissues by commercial AP‐MALDI mass spectrometry imaging (MSI).ResultsThe sensitivity of a commercial AP‐MALDI system for endogenous neuropeptides in mouse pituitary was enhanced by up to 15.2‐fold by shortening the transmission gap from the sample plate to the inlet, attaching copper adhesive tape to an indium tin oxide‐coated glass slide, optimizing the matrix spray solvent and using sample tissue washing pretreatment. Following careful optimization, the distributions of nine endogenous neuropeptides were successfully visualized in the pituitary. Furthermore, the quantitative capability of AP‐MALDI for neuropeptides was evaluated and the concentrations of neuropeptides oxytocin and vasopressin in the pituitary posterior lobe were increased approximately twofold under hypertonic saline stress.ConclusionMouse pituitary neuropeptides have emerged as important signaling molecules due to their role in stress response. This work indicates the potential of modified AP‐MALDI as a promising AP MSI method for in situ visualization and quantification of neuropeptides in complex biological tissues.

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“…21 Further, endogenous peptides can range from fewer than three to over 100 amino acids in length, 22 decreasing ionization efficiency and restricting applicability of digestive enzymes. 23 Thus, cleavage patterns remain unknown and cannot be used to guide the computational search space. EndoGenius, an optimized database searching program for a class of endogenous peptides, neuropeptides (NPs), was released earlier this year 24 and leverages amino acid motifs within its algorithm to confidently identify NPs.…”

Section: ■ Introductionmentioning

confidence: 99%

MotifQuest: An Automated Pipeline for Motif Database Creation to Improve Peptidomics Database Searching Programs

Dang,

Fields,

2024

J. Am. Soc. Mass Spectrom.

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Endogenous peptides are an abundant and versatile class of biomolecules with vital roles pertinent to the functionality of the nervous, endocrine, and immune systems and others. Mass spectrometry stands as a premier technique for identifying endogenous peptides, yet the field still faces challenges due to the lack of optimized computational resources for reliable raw mass spectra analysis and interpretation. Current database searching programs can exhibit discrepancies due to the unique properties of endogenous peptides, which typically require specialized search considerations. Herein, we present a high throughput, novel scoring algorithm for the extraction and ranking of conserved amino acid sequence motifs within any endogenous peptide database. Motifs are conserved patterns across organisms, representing sequence moieties crucial for biological functions, including maintenance of homeostasis. MotifQuest, our novel motif database generation algorithm, is designed to work in partnership with EndoGenius, a program optimized for database searching of endogenous peptides and that is powered by a motif database to capitalize on biological context to produce identifications. MotifQuest aims to quickly develop motif databases without any prior knowledge, a laborious task not possible with traditional sequence alignment resources. In this work we illustrate the utility of MotifQuest to expand EndoGenius' identification utility to other endogenous peptides by showcasing its ability to identify antimicrobial peptides. Additionally, we discuss the potential utility of MotifQuest to parse out motifs from a FASTA database file that can be further validated as new peptide drug candidates.

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Developing mass spectrometry for the quantitative analysis of neuropeptides

Cited by 10 publications

References 170 publications

Mass Spectrometry–Driven Discovery of Neuropeptides Mediating Nictation Behavior of Nematodes

Mass Spectrometry–Driven Discovery of Neuropeptides Mediating Nictation Behavior of Nematodes

Imaging and quantification of neuropeptides in mouse pituitary tissue by atmospheric pressure matrix‐assisted laser desorption/ionization mass spectrometry

MotifQuest: An Automated Pipeline for Motif Database Creation to Improve Peptidomics Database Searching Programs

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