@article {13817,
	title = {Designed affinity ligands to capture human serum albumin},
	journal = {Journal of Chromatography A},
	volume = {1583},
	year = {2019},
	pages = {88-97},
	abstract = {<p>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.</p>
},
	url = {https://www.sciencedirect.com/science/article/pii/S0021967318314195?via\%3Dihub},
	author = {dos Santos, R, and Figueiredo C, and Viecinski AC, and Pina AS, and Barbosa AJM, and Roque, A. C. A.}
}
