Designed affinity ligands to capture human serum albumin
| Autor: | Raquel Santos, Ana Sofia Pina, Aline Canani Viecinski, A. Cecília A. Roque, Carina Figueiredo, Arménio Jorge Moura Barbosa |
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| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Hsa binding Serum Albumin Human Ligands 010402 general chemistry 01 natural sciences Biochemistry Chromatography Affinity Analytical Chemistry chemistry.chemical_compound Protein purification medicine Combinatorial Chemistry Techniques Humans Disease biomarker Triazine Chromatography Triazines Chemistry Elution 010401 analytical chemistry Organic Chemistry General Medicine Human serum albumin 0104 chemical sciences body regions Human plasma Immunoglobulin G embryonic structures Synthetic ligands Protein Binding medicine.drug |
| Zdroj: | Journal of Chromatography A. 1583:88-97 |
| ISSN: | 0021-9673 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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