Related Experiment Video
Updated: Sep 13, 2025

Preparing a 68Ga-labeled Arginine Glycine Aspartate RGD-peptide for Angiogenesis
Published on: January 7, 2019
Bispecific Peptide Binds to VEGFR2 and Integrin αvβ3, Forming an Artificial Extracellular Matrix for Anti-Ocular
Ye Zhang1, Kuo Zhang2, Ling Xu1
1Department of Ophthalmology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, No.600 Yishan Road, Shanghai, 200233, China.
Abstract:
Ocular neovascularization (NV) leads to vision loss in various pathological conditions. Current therapies primarily inhibit vascular endothelial growth factor (VEGF) signaling; however, targeting additional pathways may improve outcomes. A bispecific peptide (BsPt) is developed that targets VEGFR2 and integrin αvβ3 to treat retinal neovascularization (RNV) and choroidal neovascularization (CNV) more effectively. BsPt binds to both receptors on endothelial cells (ECs) and forms nanofibrous networks on their surfaces, resulting in potent NV inhibition. In vitro, BsPt suppressed retinal EC migration and tube formation. Intravitreal BsPt injection outperformed aflibercept in mouse models of oxygen-induced retinopathy (OIR) and laser-induced CNV. RNA sequencing revealed that BsPt-induced nanofibers upregulated extracellular matrix (ECM) and cell adhesion genes, which may contribute to anti-angiogenesis and anti-leakage effects. In summary, BsPt targeting VEGFR2 and integrin αvβ3 demonstrates enhanced therapeutic potential for RNV and CNV.
More Related Videos
Related Concept Videos
Regulation of Angiogenesis and Blood Supply
Mechanism of Angiogenesis
Intracellular Signaling Affects Focal Adhesions
Some...
Overview of Cell-Matrix Interactions
Integrins
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Activation of Integrins
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...

