Evidence map›Paper›PMID 40429674›Full record

ArticleInternational journal of molecular sciences2025

A Novel KGD-Based αIIbβ3 Antagonist Prevents Arterial Thrombosis While Preserving Hemostasis and Avoiding Thrombocytopenia.

Yu-Ju Kuo, Ching-Hu Chung, Chun-Chao Chen, Ju-Chi Liu, Kuan-Rau Chiou, Joen-Rong Sheu, Woei-Jer Chuang, Tur-Fu Huang

Abstract read
In one paragraph

Article in International journal of molecular sciences, 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

8 authors.

Yu-Ju KuoDivision of Cardiology, Department of Internal Medicine, Shuang Ho Hospital, Taipei Medical University, Taipei 23561, Taiwan.
Ching-Hu ChungDepartment of Medicine, Mackay Medical College, New Taipei City 252, Taiwan.ORCID 0000-0002-3096-8974
Chun-Chao ChenDivision of Cardiology, Department of Internal Medicine, Shuang Ho Hospital, Taipei Medical University, Taipei 23561, Taiwan.ORCID 0000-0002-4888-3709
Ju-Chi LiuDivision of Cardiology, Department of Internal Medicine, Shuang Ho Hospital, Taipei Medical University, Taipei 23561, Taiwan.
Kuan-Rau ChiouDivision of Cardiology, Department of Internal Medicine, Shuang Ho Hospital, Taipei Medical University, Taipei 23561, Taiwan.
Joen-Rong SheuGraduate Institute of Medical Sciences, College of Medicine, Taipei Medical University, Taipei 11031, Taiwan.ORCID 0000-0001-8265-3678
Woei-Jer ChuangDepartment of Biochemistry, National Cheng Kung University Medical College, Tainan 701, Taiwan.
Tur-Fu HuangDepartment of Medicine, Mackay Medical College, New Taipei City 252, Taiwan.

Funding

National Science and Technology Council NSTC 113-2311-B-006-002
6 · The paper itself

Abstract

Current αIIbβ3 antagonists are potent antithrombotic agents, their clinical use is limited by the risk of life-threatening bleeding. Emerging evidence has highlighted key mechanistic differences between thrombosis and hemostasis, opening avenues for safer antithrombotic strategies. Targeting integrin αIIbβ3 outside-in signaling has been proposed to mitigate bleeding risk; however, the short half-life of peptide-based therapeutics remains a major challenge. In this study, we developed an optimized αIIbβ3 antagonist, KGDRR-a recombinant mutant protein derived from snake venom disintegrin, incorporating an Arg55 residue within the KGD loop-through systematic structure-activity relationship (SAR) analysis. Molecular docking revealed a critical cation-π interaction between Arg55 of KGDRR and Tyr122 of the β3 subunit, stabilizing integrin αIIbβ3 in an unliganded-closed conformation. Functionally, KGDRR selectively inhibited thrombus propagation by blocking ligand binding and downstream Gα13-mediated outside-in signaling while preserving initial thrombus core formation, which is a limitation of current αIIbβ3 inhibitors. Unlike conventional antagonists, KGDRR maintained αIIbβ3 in an unliganded-closed conformation without inducing the integrin activation and conformational change that lead to immune-mediated platelet clearance and thrombocytopenia. In animal models, KGDRR effectively suppressed thrombus growth without causing thrombocytopenia or prolonging bleeding time. Furthermore, intramuscular administration of KGDRR achieved a functional half-life 3.5 times longer than that of the clinically used antithrombotic eptifibatide at equivalent antithrombotic efficacy. In conclusion, KGDRR exhibits potent antithrombotic activity with a favorable safety profile and enhanced pharmacokinetic stability. These findings position KGDRR as a promising next generation αIIbβ3 antagonist with the potential to improve clinical outcomes in antithrombotic therapy.

Indexed as

DisintegrinsFibrinolytic AgentsHemostasisPlatelet Aggregation InhibitorsPlatelet Glycoprotein GPIIb-IIIa ComplexThrombocytopeniaThrombosisAnimalsDisease Models, AnimalHumansMaleMiceMolecular Docking SimulationStructure-Activity RelationshipDisintegrinsFibrinolytic AgentsPlatelet Aggregation InhibitorsPlatelet Glycoprotein GPIIb-IIIa Complexbi-directional signalingbinding sitesdisintegrinhemorrhagic riskintegrin αIIbβ3thrombosis

Identifiers

PMID40429674
PMCPMC12111684

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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.