Evidence map›Paper›PMID 40764671›Full record

ReviewNature protocols2026

Mass spectrometry-based top-down proteomics for proteoform profiling of protein coronas.

Seyed Amirhossein Sadeghi, Fei Fang, Reyhane Tabatabaeian Nimavard, Qianyi Wang, Guijie Zhu, Amir Ata Saei, Liangliang Sun, Morteza Mahmoudi

Abstract readReview
In one paragraph

Review in Nature protocols, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. A Draft Map of E. coli Proteoforms.Analytical chemistry · 2026
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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

8 authors.

Seyed Amirhossein Sadeghi *Department of Chemistry, Michigan State University, East Lansing, MI, USA.
Fei Fang *Department of Chemistry, Michigan State University, East Lansing, MI, USA.ORCID 0000-0003-0829-9871
Reyhane Tabatabaeian NimavardDepartment of Chemistry, Michigan State University, East Lansing, MI, USA.
Qianyi WangDepartment of Chemistry, Michigan State University, East Lansing, MI, USA.
Guijie ZhuDepartment of Chemistry, Michigan State University, East Lansing, MI, USA.
Amir Ata SaeiDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institute, Stockholm, Sweden.
Liangliang SunDepartment of Chemistry, Michigan State University, East Lansing, MI, USA. lsun@chemistry.msu.edu.
Morteza MahmoudiPrecision Health Program, Michigan State University, East Lansing, MI, USA. mahmou22@msu.edu.ORCID 0000-0002-2575-9684

Funding

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
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 R35 GM153479U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI) R01CA247863U.S. Department of Health & Human Services | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (National Institute of Diabetes & Digestive & Kidney Diseases) DK131417U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM153479
6 · The paper itself

Abstract

The protein corona is a layer of biomolecules-primarily proteins-that adsorbs to nanoparticle (NP) surfaces in biological fluids. If the purpose of the NP is therapeutic, this can have a profound effect on its biological activity and function in vivo. Protein corona formation can also be exploited for diagnostic purposes and to differentially enrich proteins for biomarker discovery. For all of these applications, it is useful to determine which proteins, and which specific proteoforms, bind to different types of NP. The traditional mass spectrometry (MS)-based bottom-up proteomics does not accurately identify specific proteoforms within the protein corona. This limitation impedes the nanomedicine field's ability to precisely predict the biological fate and pharmacokinetics of nanomedicines and their effectiveness in early-stage biomarker discovery and disease detection because many different proteoforms of the same gene could exist in the corona, and they have divergent biological functions. Here, we describe how to use capillary zone electrophoresis (CZE)-MS-based top-down proteomics to characterize the proteoform landscape of the protein corona. Our procedures detail the recovery of intact proteoforms from NP surfaces by using detergent-assisted proteoform elution and the measurement of these proteoforms by using CZE-tandem MS (MS/MS) and CZE-high-field asymmetric waveform ion mobility spectrometry (FAIMS)-MS/MS. The entire workflow is completed within 3-4 d. Using this protocol, hundreds of proteoforms from the protein corona of polystyrene NPs can be identified. Distinct protein corona proteoform profiles were observed from NPs with different physicochemical properties. The addition of FAIMS is beneficial for more in-depth proteoform characterization.

Indexed as

Mass SpectrometryProtein CoronaProteomicsElectrophoresis, CapillaryHumansNanoparticlesProtein Corona

Identifiers

PMID40764671
PMCPMC12407567

What Socratic holds

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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 Socratic graph.