Designed affinity ligands to capture human serum albumin
- Citation:
- dos Santos, R, Figueiredo C, Viecinski AC, Pina AS, Barbosa AJM, Roque ACA. 2019. Designed affinity ligands to capture human serum albumin. Journal of Chromatography A. 1583:88-97.
Abstract:
Human serum albumin (HSA) in an important therapeutic agent and disease biomarker, with an increasing market demand. By proteins and drugs that bind to HSA as inspiration, a combinatorial library of 64 triazine-based ligands was rationally designed and screened for HSA binding at physiological conditions. Two triazine-based lead ligands (A3A2 and A6A5), presenting more than 50% HSA bound and high enrichment factors, were selected for further studies. Binding and elution conditions for HSA purification from human plasma were optimized for both ligands. The A6A5 adsorbent yielded a purified HSA sample with 98% purity at 100% recovery yield under mild binding and elution conditions.
