Evidence map›Paper›PMID 41820789›Full record

ArticleProtein science : a publication of the Protein Society2026

AI-assisted design of a VEGFR2 agonistic peptide that promotes angiogenesis and wound repair.

Farzana Yasmeen, Rajath Ramachandran, Rameez Hassan Pirzada, Bogeum Choi, Hana Seo, Wook Kim, Moon Suk Kim, Sangdun Choi

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. 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. AI-assisted design of a VEGFR2 agonistic peptide that promotes angiogenesis and wound repair.Protein science : a publication of the Protein Society · 2026
    Article
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.

Farzana YasmeenDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Rajath RamachandranDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Rameez Hassan PirzadaDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Bogeum ChoiDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Hana SeoDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Wook KimDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Moon Suk KimDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.
Sangdun ChoiDepartment of Molecular Science and Technology, Ajou University, Suwon, Republic of Korea.ORCID https://orcid.org/0000-0001-5920-7848

Funding

National Research Foundation of Korea NRF-2019M3D1A1078938National Research Foundation of Korea NRF-2022M3A9G1014520National Research Foundation of Korea NRF-2023R1A2C2003034
6 · The paper itself

Abstract

Vascular endothelial growth factor (VEGF) serves as a principal regulator of neovascularization and is essential for vascular regeneration. In this study, we identified and evaluated VEGF Mimetic Peptide3 (VMP3), a novel synthetic peptide developed as a potential VEGFR-2/VEGF-A modulator. VMP3 was generated using an AI-assisted peptide design framework incorporating long short-term memory (LSTM) networks, which enabled learning of sequence-level patterns within known VEGF agonist peptides and assisted the motif-guided and structure-informed design of new candidates. Molecular dynamics simulations suggested a stable interaction profile between VMP3 and VEGFR2, supporting the feasibility of receptor engagement. Experimental validation was performed using in vitro, ex vivo, and in vivo methods. In vitro functional assays showed that VMP3 promoted endothelial cell proliferation, migration, and invasion in a manner similar to that of native VEGF. Ex vivo aortic ring assays supported these findings, demonstrating micro vessel sprouting following VMP3 treatment. An in vivo Matrigel plug assay in C57BL/6J mice revealed increased neovascularization following VMP3 treatment, as confirmed by histological and immunohistochemical analyses (H&E and CD31 staining). In addition, in a diabetic mouse wound healing model, VMP3 significantly accelerated wound closure, and tissue-level analysis of wound sites confirmed enhanced re-epithelialization and neovascularization, as evidenced by Masson's trichrome, Picrosirius Red, H&E, and CD31 staining. Collectively, these results suggested that VMP3 functions in a manner similar to that of VEGF, promoting angiogenesis.

Indexed as

AngiogenesisNeovascularization, PhysiologicPeptidesVascular Endothelial Growth Factor Receptor-2Wound HealingAnimalsCell MovementCell ProliferationHumansHuman Umbilical Vein Endothelial CellsMiceMice, Inbred C57BLMolecular Dynamics SimulationVascular Endothelial Growth Factor AKDR protein, humanPeptidesVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2angiogenesismolecular modelingpeptide therapeuticsVEGFR2 agonistwound repair

Identifiers

PMID41820789
PMCPMC13140732

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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.