ArticleACS nano2025
In Situ Metal-Organic Framework Growth in Serum Encapsulates and Depletes Abundant Proteins for Integrated Plasma Proteomics.
Article in ACS nano, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Biomacromolecule-MOF Composites for Intracellular Delivery: From Empirical Construction to Rational Design and AI-Assisted Screening.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
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Authors and funding
7 authors.
Funding
Abstract
Protein biomarkers in human serum provide critical insights into various physiological conditions and diseases, enabling early diagnosis, prognosis, and personalized treatment. However, detecting low-abundance protein biomarkers is challenging due to the presence of highly abundant proteins that make up ∼99% of the plasma proteome. Here, we report the use of in situ metal-organic framework (MOF) growth in serum to effectively deplete highly abundant serum proteins for integrated proteomic analysis. Through biomolecule-mediated nucleation of a zeolitic imidazolate framework (ZIF-8), abundant plasma proteins are selectively encapsulated within ZIF-8 and removed from serum via centrifugation, leaving a depleted protein fraction in the supernatant. Bottom-up proteomics analysis confirmed significant depletion of the topmost abundant proteins, many at depletion levels exceeding 95%. Such depletion enabled the identification of 277 total proteins in the supernatant (uncaptured) fraction in a single-shot analysis, including 54 proteins that were only identified after depletion, 12 drug targets, and many potential disease biomarkers. Top-down proteomics characterization of the captured and uncaptured protein fractions at the proteoform-level confirmed this method is not biased toward any specific proteoform of individual proteins. These results demonstrate that in situ MOF growth can selectively and effectively deplete high-abundance proteins from serum in a simple, low cost, one-pot synthesis to enable integrated top-down and bottom-up proteomic analysis of serum protein biomarkers.
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