Aflibercept differs from ranibizumab and bevacizumab in its mechanism of anti-VEGF action because aflibercept:
- A Is a recombinant fusion protein that binds VEGF-A, VEGF-B, and placental growth factor (PlGF) with higher affinity than ranibizumab ✓
- B Is a humanized monoclonal antibody fragment targeting VEGF-A only
- C Acts via RNA interference to inhibit VEGF synthesis intracellularly
- D Inhibits VEGF receptor tyrosine kinase activity on endothelial cells
Explanation
Aflibercept (VEGF Trap, Eylea) is a recombinant fusion protein containing extracellular domains of VEGFR-1 (domain 2) and VEGFR-2 (domain 3) fused to the Fc portion of IgG1. It acts as a 'decoy receptor' binding VEGF-A, VEGF-B, and PlGF with picomolar affinity — approximately 100-fold higher than ranibizumab for VEGF-A. Ranibizumab is a Fab fragment of a humanized anti-VEGF-A monoclonal antibody. Bevacizumab is a full-length humanized monoclonal antibody targeting VEGF-A. RNA interference is the mechanism of bevasiranib (discontinued). Receptor tyrosine kinase inhibition is the mechanism of systemic anti-VEGF small molecules.
Reference: Khurana Comprehensive Ophthalmology, 7th ed.
High-yield for: NEET PGINI-CETNExTFMGEUSMLEPLABMRCP
Written and medically reviewed by the StethoPrep medical team.