DR10601 is a glucagon receptor (GCGR)/GLP-1 receptor (GLP-1R) dual agonist covalently linked to an Fc fragment of human IgG4. To develop safe and potent dual-agonists or tri-agonists for the treatment of obesity, NASH and T2DM, great efforts have been made to screen hybrid peptides with balanced potency for GCGR,GLP-1R and/or GIPR in the past years. Most of these hybrid peptides are lipidated or pegylated for the purpose of less susceptible to metabolic degradation and renal clearance. DR10601,however,is designed to fuse with Fc fragment of human IgG4. Preclinical experiments demonstrated that DR10601 has significant in vitro GCGR/GLP-1R activities and superior weight loss and hypoglycemic effects in vivo.
DR10619 is another superior alternative for the treatment of obesity, NASH and T2DM in our pipeline. Besides GCGR and GLP-1R, DR10619 also targets FGFR1/KLB, as it includes a FGF-21 analogue in the C terminal.FGF-21 and FGF-21 analogue are promising drug candidates for the treatment of T2DM, with superior potency in maintenance of glucose, lipid and energy homeostasis. FGF-21 analogue shows a synergistic effect in weight loss and blood glucose control when fused with DR10601, which indicates a potential reduced dose and improved safety.
DR10406 is a varant of FGF-21 fused to Fc fragment of human IgG. DR10406 is engineered to combination administration with DR10601 in therapy of obesity,NASH and T2DM.
DR50102 is a AccuBody® technology based anti-CEA/CD3 antibody derivative developed for oncotherapy. DR50102 is characteristic of a protease cleavage site susceptible to specific proteases unique to the tumor microenvironment, which is inserted between the anti-CD3 Fab and xLONG® sequence. Following cleavage, the bispecific anti-CEA/CD3 antibody will be accurately activated due to escape from the shield of xLONG®. As AccuBody restrict T-cell recruiting activity to tumor microenvironment, it is potentially superior to other formats of therapeutic regimens considering its improved safety.
DR50201 is another AccuBody® technology derived antibody targeting EGFR developed for oncotherapy. DR50201 also contains a protease cleavage site susceptible to specific proteases unique to the tumor microenvironment, which is inserted between the anti-EGFR antibody and xLONG® sequence. Following cleavage, the anti-EGFR activity will be accurately released due to escape from the shield of xLONG® .
In DR30121,a xLONG® fragment is added to the Fc fusion protein targeting VEGF and Angiopoietin-2(Ang-2).The vitreous half-life of DR30121 is significantly prolonged due to fusion of xLONG®. DR30121 is intent to extend intravitreal administration beyond monthly (ranibizumab) or bimonthly (aflibercept)labels, which could possibly increase patient/provider compliance and relieve patient burden with ocular diseases like AMD.
DR10505 is human Arginase I（hArg I）derived best-in-class biotherapeutics based on xLONGylation®. We screened a series of xLONG® fragments with different length and sequence to improve the in vivo pharmacokinetic profile of hArg I, which is reported as trimeric metalloenzyme. hArg I has been developed for hyperargininemia and cancer therapy by pegylation in recent years. Althougth the trimeric hArg I has a apparent molecular weight above 100 KDa, its observed half life is relatively short (about 5 hours) for unknown reasons. Instead of chemically conjugated with PEGs, hArg I is recombinantly fused with xLONG® sequence for pharmacokinetic improvement during development .