Evidence map›Paper›PMID 41518121›Full record

ArticleJournal of separation science2026

A Polymeric Zwitterionic Hydrophilic Probe for Mapping the Human Serum Endogenous Glycopeptidome.

Muhammad Salman Sajid, Shafaq Saleem, Habtom W Ressom

Abstract read
In one paragraph

Article in Journal of separation science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Muhammad Salman SajidDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC, USA.
Shafaq SaleemDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC, USA.
Habtom W RessomDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington, DC, USA.

Funding

Systems Metabolomics for Biomarker DiscoveryR35GM141944 · NIGMS · GEORGETOWN UNIVERSITY · PI RESSOM, HABTOM W · 2021 to 2025
$2.4M
NIGMS NIH HHS R35 GM141944of the National Institutes of Health R35GM141944
6 · The paper itself

Abstract

Endogenous glycopeptides in human serum are valuable candidates for disease biomarker discovery, but their low abundance and structural complexity pose significant analytical challenges. In this study, we developed and optimized a robust workflow for enriching and in-depth characterizing the endogenous glycopeptidome using a novel hydrophilic interaction liquid chromatography (HILIC) sorbent. The HILIC-based strategy effectively enriched glycopeptides from mono-glycosylated IgG and avidin digests, as well as multi-glycosylated horseradish peroxidase (HRP), demonstrating high selectivity, femtomolar-level sensitivity (down to 1 fmol), reproducibility (RSD > 1), and reusability for up to four cycles. Comprehensive analysis by mass spectrometry (MS) identified 334 endogenous intact N-linked glycopeptides, including 318 N-glycosites from 289 glycoproteins. In addition, 242 endogenous intact O-linked glycopeptides from 38 glycoproteins are identified. These represent one of the most extensive endogenous glycopeptide datasets to date. N-glycans were primarily complex biantennary types, while Core 1 structures dominated O-glycans. Motif analysis revealed a strong preference for canonical N-glycosylation motifs (NXT/NXS) and a nearly equal distribution of O-glycosylation on serine and threonine residues. Gene Ontology analysis indicated functional enrichment in membrane-associated, catalytic, and immune-related processes. This optimized HILIC-MS platform enables sensitive and reproducible glycoproteomic profiling, providing a valuable tool for biomarker discovery.

Indexed as

GlycopeptidesGlycoproteinsPolymersChromatography, LiquidGlycosylationHumansHydrophobic and Hydrophilic InteractionsGlycopeptidesGlycoproteinsPolymersendogenous glycopeptidomeenrichmenthuman serummass spectrometrypolymeric zwitterionic hydrophilic probe

Identifiers

PMID41518121
PMCPMC12831618

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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.