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.
| Original language | English |
|---|---|
| Pages (from-to) | 88-97 |
| Journal | Journal Of Chromatography A |
| Volume | 1583 |
| DOIs | |
| Publication status | Published - 4 Jan 2019 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Affinity ligands
- Combinatorial chemistry
- Human serum albumin
- Protein purification
- Synthetic ligands
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