4.6 Article

Designed affinity ligands to capture human serum albumin

期刊

JOURNAL OF CHROMATOGRAPHY A
卷 1583, 期 -, 页码 88-97

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.chroma.2018.11.021

关键词

Protein purification; Human serum albumin; Synthetic ligands; Affinity ligands; Combinatorial chemistry

资金

  1. Unidade de Ciencias Biomoleculares Aplicadas, UCIBIO
  2. national funds from FCT/MEC [UID/Multi/04378/2013]
  3. ERDF under the PT2020 Partnership Agreement [POCI-01-0145-FEDER-007728]
  4. PhD program Molecular Biosciences [PD/BD/105753/2014, PD/00133/2012]
  5. Post-Doc fellowship [SFRH/BPD/97585/2013, SFRH/BPD/112543/2015]
  6. Fundação para a Ciência e a Tecnologia [PD/BD/105753/2014] Funding Source: FCT

向作者/读者索取更多资源

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. (C) 2018 Elsevier B.V. All rights reserved.

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