ArticleJournal of ophthalmic & vision research2026
Article in Journal of ophthalmic & vision research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Purpose: Blocking the interaction between vascular endothelial growth factor (VEGF) and vascular endothelial growth factor receptor-2 (VEGFR2) is recognized as an effective strategy for treating neovascular age-related macular degeneration (nAMD). The present research aimed at designing and modelling an anti-VEGF peptide based on ranibizumab for potential application in inhibiting the VEGF/VEGFR2 interaction. Methods: Effective amino acids in the interaction between VEGF and ranibizumab were analyzed using Swiss-PdbViewer (SPDBV), PyMOL, and Chimera software. The effective area in this interaction was determined and applied as a basis to design a peptide. Then, this sequence (containing 25 amino acids) was subjected to random mutagenesis, and the binding affinity of the resulting peptides was analyzed using the ClusPro software. Subsequently, GROMACS v5.0.6 was employed for molecular dynamics (MD) simulations to evaluate the stability of target-ligand complexes. Ultimately, the peptide exhibiting the highest affinity was grafted into the kB1 and MCoTI-II frameworks to enhance the stability. Results: This modification resulted in improved peptide-VEGF binding affinity, demonstrating the potential of Conclusion: The findings from this study provide a basis for designing and validating peptide inhibitors against VEGF.
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Registered trials
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 Socratic graph.