Evidence map›Paper›PMID 39276099›Full record

ArticleACS nano2024

Mass Spectrometry-Based Top-Down Proteomics in Nanomedicine: Proteoform-Specific Measurement of Protein Corona.

Seyed Amirhossein Sadeghi, Ali Akbar Ashkarran, Qianyi Wang, Guijie Zhu, Morteza Mahmoudi, Liangliang Sun

Abstract read
In one paragraph

Article in ACS nano, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Review
  2. A Draft Map of E. coli Proteoforms.Analytical chemistry · 2026
    Article
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  14. Review
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  18. Review
  19. Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
  20. 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

6 authors.

Seyed Amirhossein SadeghiDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan 48824, United States.
Ali Akbar AshkarranDepartment of Radiology and Precision Health Program, Michigan State University, East Lansing, Michigan 48824, United States.
Qianyi WangDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan 48824, United States.
Guijie ZhuDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan 48824, United States.
Morteza MahmoudiDepartment of Radiology and Precision Health Program, Michigan State University, East Lansing, Michigan 48824, United States.ORCID 0000-0002-2575-9684
Liangliang SunDepartment of Chemistry, Michigan State University, 578 S Shaw Lane, East Lansing, Michigan 48824, United States.ORCID 0000-0001-8939-5042

Funding

Computational tools for top down mass spectrometry based proteoform identification and proteogenomicsR01GM118470 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI Xiaowen Liu · 2016 to 2026
$2.7M
A Nanostructured Skin Patch to Heal Chronic WoundsR01DK131417 · NIDDK · MICHIGAN STATE UNIVERSITY · PI Morteza Mahmoudi · 2022 to 2026
$2.0M
Quantitative top-down proteomics of human colorectal cancer cells and tumorsR01CA247863 · NCI · MICHIGAN STATE UNIVERSITY · PI HUMMON, AMANDA B., LIU, XIAOWEN · 2021 to 2025
$1.9M
Quantitative proteomics of Zebrafish embryos and blastomeresR01GM125991 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SUN, LIANGLIANG · 2018 to 2022
$1.7M
Advancing top-down proteomics with capillary electrophoresis-mass spectrometryR35GM153479 · NIGMS · MICHIGAN STATE UNIVERSITY · PI Liangliang Sun · 2024 to 2026
$1.4M
NCI NIH HHS R01 CA247863NIDDK NIH HHS R01 DK131417NIGMS NIH HHS R01 GM118470NIGMS NIH HHS R01 GM125991NIGMS NIH HHS R35 GM153479
6 · The paper itself

Abstract

Conventional mass spectrometry (MS)-based bottom-up proteomics (BUP) analysis of the protein corona [i.e., an evolving layer of biomolecules, mostly proteins, formed on the surface of nanoparticles (NPs) during their interactions with biomolecular fluids] enabled the nanomedicine community to partly identify the biological identity of NPs. Such an approach, however, fails to pinpoint the specific proteoforms─distinct molecular variants of proteins in the protein corona. The proteoform-level information could potentially advance the prediction of the biological fate and pharmacokinetics of nanomedicines. Recognizing this limitation, this study pioneers a robust and reproducible MS-based top-down proteomics (TDP) technique for characterizing proteoforms in the protein corona. Our TDP approach has successfully identified about 900 proteoforms in the protein corona of polystyrene NPs, ranging from 2 to 70 kDa, revealing proteoforms of 48 protein biomarkers with combinations of post-translational modifications, signal peptide cleavages, and/or truncations─details that BUP could not fully discern. This advancement in MS-based TDP offers a more advanced approach to characterize NP protein coronas, deepening our understanding of NPs' biological identities. We, therefore, propose using both TDP and BUP strategies to obtain more comprehensive information about the protein corona, which, in turn, can further enhance the diagnostic and therapeutic efficacy of nanomedicine technologies.

Indexed as

biomarker discoverymass spectrometrynanomedicineprotein coronaproteoformtop-down proteomics

Identifiers

PMID39276099
PMCPMC11440641

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Registered trials

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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.