Evidence map›Paper›PMID 40780635›Full record

ArticleActa biomaterialia2025

Fatty acid albumin conjugates mechanically weaken and disrupt degradation of fibrin networks.

Yujen Wang, Sajjad Norouzi, Arsalan Nisar, Justin Houser, Sachin Kumar, Mohammadhasan Hedayati, H Samet Varol, Paula Delgado, Naomi Calhoun, Leah Gutzwiller and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta biomaterialia, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

13 authors.

Yujen WangDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
Sajjad NorouziDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
Arsalan NisarDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
Justin HouserDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
Sachin KumarAll India Institute of Medical Sciences, Ansari Nagar, New Delhi, 110029, India; Centre for Biomedical Engineering, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, 110016, India.
Mohammadhasan HedayatiDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
H Samet VarolDepartment of Chemistry "Giacomo Ciamician", Università degli Studi di Bologna, Via Selmi 2, 40126 Bologna, Italy.
Paula DelgadoDepartment of Metallurgical Materials, and Biomedical, Engineering, The University of Texas at El Paso, El Paso, TX 79968, USA.
Naomi CalhounDepartment of Chemical Engineering, Howard University, Washington DC, DC 20059, USA.
Leah GutzwillerDepartment of Biomedical/Medical Engineering, University of Tennessee, Knoxville, TN 37996, USA.
Jeanne C StachowiakDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA; Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
Manuel K RauschDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA; Department of Aerospace Engineering and Engineering Mechanics, University of Texas at Austin, TX 78712, USA.
Sapun H ParekhDepartment of Biomedical Engineering, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: sparekh@utexas.edu.

Funding

Phase II of BUILDing SCHOLARSUL1GM118970 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI ALEY, STEPHEN B, BOLAND, THOMAS · 2015 to 2023
$17.9M
Phase II of BUILDing SCHOLARS - Student Training CoreTL4GM118971 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI ALEY, STEPHEN B, BOLAND, THOMAS · 2015 to 2023
$9.9M
Phase II of BUILDing SCHOLARS - Research Enrichment CoreRL5GM118969 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI ALEY, STEPHEN B, BOLAND, THOMAS · 2015 to 2023
$7.4M
Protein Networks as Synergistic Drivers of Membrane RemodelingR35GM139531 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Jeanne Casstevens Stachowiak · 2021 to 2026
$4.0M
National Science Foundation 2105175NIGMS NIH HHS R35 GM139531NIGMS NIH HHS RL5 GM118969NIGMS NIH HHS TL4 GM118971NIGMS NIH HHS UL1 GM118970NIH HHS UL1GM118970NIH National Institutes of Health R35GM139531NIH National Institutes of Health RL5GM118969NIH National Institutes of Health TL4GM118971
6 · The paper itself

Abstract

Cardiovascular diseases and stroke together account for the largest causes of death in Western countries. These pathologies are directly linked to the formation of blood clots that block blood flow to vital organs. Common risk factors for such clots are obesity, high blood pressure, diabetes, and high LDL cholesterol. Immediate thrombolytic treatment to dissolve fibrin-rich clots can save lives, but recent research has shown that pure fatty acids (FA) can inhibit thrombolysis via interaction with plasmin. However, since FAs are often complexed to serum albumin in the blood, it is unclear how FAs in blood interact with plasmin, or perhaps with clots, to modulate thrombolysis. Here, we studied how elevated levels of two abundant FAs (oleic and palmitic acid) complexed to bovine serum albumin (BSA) affect fibrin hydrogels and their degradation. We observed the binding of fatty acid-BSA (FABSA) conjugates to fibrin via Förster resonance energy transfer microscopy and noted the effects of FABSA on fibrin gels mechanics and fibrinolysis compared to pure fibrin networks. Specifically, with FABSA in the fibrin network, fibrin hydrogels were mechanically weakened and showed a significant decrease in fibrinolysis speed. These studies show that elevated fatty acid content modifies clot properties, making them mechanically weaker and more resistant to degradation. STATEMENT OF SIGNIFICANCE: Fibrin networks are the primary load-bearing element in blood clots, which are subject to various cyclic forces in the body and have excellent mechanical properties resulting from fibrin's hierarchical structure. These networks are formed in the presence fatty acids, lipoproteins, and albumin in the blood; however, little is known about how these additional constituents modify fibrin network properties. By imaging protein fiber orientation, molecular structure, and degradation in situ, we find that fibrin formation in the presence of elevated fatty acids conjugated to albumin modifies network structure, mechanically weakens fibrin networks, and slows fibrin network degradation considerably. Based on our findings, we suspect that increased fat in blood may lead impeded fibrin degradation and increased clot persistence.

Indexed as

Fatty AcidsFibrinProteolysisSerum Albumin, BovineAnimalsCattleFibrinolysisHumansHydrogelsFatty AcidsFibrinHydrogelsSerum Albumin, BovineDegradationECMECM mechanicsFatty acidsFibrin clots

Identifiers

PMID40780635
PMCPMC13481148

What OpenQuestion holds

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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.