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