Evidence map›Paper›PMID 36921255›Full record

ArticleJournal of proteome research2023

Definitive Screening Designs to Optimize Library-Free DIA-MS Identification and Quantification of Neuropeptides.

Ashley Phetsanthad, Austin V Carr, Lauren Fields, Lingjun Li

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.1field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Origins, Technological Advancement, and Applications of Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Ashley PhetsanthadDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0001-9038-1107
Austin V CarrDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0001-6595-3476
Lauren FieldsDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0001-8155-642X
Lingjun LiDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0003-0056-3869
University of Wisconsin–Madison · US

Funding

Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
Creating a region- specific biomolecular atlas of the brain of Alzheimer’s diseaseR01AG078794 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI, Luigi Puglielli · 2022 to 2026
$3.7M
Di-Leu-enabled multiplexed quantitation for biomarker discovery and validation in Alzheimer's diseaseRF1AG052324 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2018 to 2018
$2.4M
Acquisition of a High-Field Dual Source FTICR-MS for Pharmaceutical ResearchS10RR029531 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2011 to 2011
$2.1M
Mass Spectrometry Investigations into the Glycosylated Neuropeptidome in Response to Hypoxic StressF31GM143916 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PHETSANTHAD, ASHLEY · 2022 to 2022
$34k
NCRR NIH HHS S10 RR029531NIA NIH HHS R01 AG078794NIA NIH HHS RF1 AG052324NIDDK NIH HHS R01 DK071801NIGMS NIH HHS F31 GM143916NIGMS NIH HHS T32 GM008505
6 · The paper itself

Abstract

Method optimization is crucial for successful mass spectrometry (MS) analysis. However, extensive method assessments, altering various parameters individually, are rarely performed due to practical limitations regarding time and sample quantity. To maximize sample space for optimization while maintaining reasonable instrumentation requirements, a definitive screening design (DSD) is leveraged for systematic optimization of data-independent acquisition (DIA) parameters to maximize crustacean neuropeptide identifications. While DSDs require several injections, a library-free methodology enables surrogate sample usage for comprehensive optimization of MS parameters to assess biomolecules from limited samples. We identified several parameters contributing significant first- or second-order effects to method performance, and the DSD model predicted ideal values to implement. These increased reproducibility and detection capabilities enabled the identification of 461 peptides, compared to 375 and 262 peptides identified through data-dependent acquisition (DDA) and a published DIA method for crustacean neuropeptides, respectively. Herein, we demonstrate a DSD optimization workflow, using standard material, not reliant on spectral libraries for the analysis of any low abundance molecules from previous samples of limited availability. This extends the DIA method to low abundance isoforms dysregulated or only detectable in disease samples, thus improving characterization of previously inaccessible biomolecules, such as neuropeptides. Data are available via ProteomeXchange with identifier PXD038520.

Indexed as

NeuropeptidesProteomicsMass SpectrometryPeptidesProteomeReproducibility of ResultsNeuropeptidesPeptidesProteomedata-independent acquisitiondesign of experimentsDIAlabel-free quantitationneuropeptidespeptidomics

Identifiers

PMID36921255
PMCPMC10190159
OpenAlexW4324326953

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.