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Identification of VEGFR2-binding peptides using high throughput bacterial display methods and functional assessment
Kefeng Pu, Lihua Yuan, Lisha Chen
1398 Ruoshui Road, Suzhou Industrial Park, Suzhou 215123, China. ymzhu2008@sinano.ac.cn.
Current Cancer Drug Targets
|March 31, 2015
Summary
Researchers developed a high-affinity peptide, VRBP1, that targets vascular endothelial growth factor receptor 2 (VEGF-VEGFR2). This peptide effectively reduced tumor size in preclinical models, showing potential for cancer therapy.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Vascular endothelial growth factor-vascular endothelial growth factor receptor 2 (VEGF-VEGFR2) signaling is crucial for tumor angiogenesis.
- Targeting VEGFR2 offers a therapeutic strategy for malignant cancers.
Purpose of the Study:
- To identify and characterize high-affinity VEGFR2-binding peptides for potential cancer therapy.
- To evaluate the therapeutic efficacy of a selected peptide, VRBP1, in preclinical cancer models.
Main Methods:
- Bacterial display technology was employed to screen for specific VEGFR2-binding peptides.
- Surface plasmon resonance (SPR) assays determined binding affinity (KD) and competition with VEGF.
- In vivo xenograft models and immunohistochemical analysis assessed therapeutic effects.
Main Results:
- A conserved motif (FF/YEXWGVK) was identified in selected peptides.
- VRBP1 demonstrated high affinity (KD = 228.3 nM) for VEGFR2 and competed with VEGF binding.
- VRBP1-conjugated particles recognized VEGFR2-expressing cells (HUVEC).
- In vivo studies showed VRBP1 significantly reduced tumor size and decreased CD31 expression in H460 xenografts.
Conclusions:
- VEGFR2-binding peptides, exemplified by VRBP1, hold significant potential as therapeutic agents for cancer.
- These peptides can be utilized for both cancer diagnosis and therapy due to their specific targeting capabilities.
