A Novel Full-Length Recombinant Human Complement Factor H (CFH; GEM103) for the Treatment of Age-Related Macular Degeneration Shows Similar <i>In Vitro</i> Functional Activity to Native CFH
Robyn M. Biggs, Elisavet Makou, Scott Lauder, Andrew P. Herbert, Paul N. Barlow, Suresh Katti
Abstract
PURPOSE: . This study aimed to investigate the complement pathway-related functions of GEM103 in comparison with those of native human CFH. METHODS: Key biological activities of GEM103 and human serum-derived CFH (sdCFH) were compared using four independent functional assays. Assays of C3b binding and C3 convertase decay-accelerating activity (DAA) were performed by surface plasmon resonance (SPR). Cofactor activity (CA) was measured using 8-anilinonaphthalene-1-sulfonic acid as a fluorescent probe of C3b integrity. The abilities of GEM103 and sdCFH to protect sheep erythrocytes from hemolysis by CFH-depleted normal human serum were assessed colorimetrically. RESULTS: = 0.81). CONCLUSIONS: functional activity. These results support further study of GEM103 as a potential therapy for AMD.