![]() Peptides combine a range of favourable qualities such as suitable affinity and selectivity, low inherent toxicity, and access to chemical synthesis which make them an attractive modality for therapeutic development 1. This high-affinity albumin ligand could potentially extend the half-life of peptides in human to several days, substantially broadening the application range of peptides as therapeutics. Conjugation to a peptide factor XII inhibitor developed for anti-thrombotic therapy extends the half-life from 13 minutes to over five hours, inhibiting coagulation for eight hours in rabbits. This ligand prolongs the elimination half-life of cyclic peptides in rats 25-fold to over seven hours. ![]() In accordance with this strategy, we developed an easily synthesized albumin-binding ligand based on a peptide-fatty acid chimera that has a high affinity for human albumin ( K d=39 nM). An intriguing approach for extending peptide circulation times works through a ‘piggy-back’ strategy in which peptides bind via a ligand to the long-lived serum protein albumin. The rapid renal clearance of peptides in vivo limits this attractive platform for the treatment of a broad range of diseases that require prolonged drug half-lives. ![]()
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