Designed affinity ligands to capture human serum albumin

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1 Citation (Scopus)

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 languageEnglish
Pages (from-to)88-97
JournalJournal Of Chromatography A
Volume1583
DOIs
Publication statusPublished - 4 Jan 2019

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Serum Albumin
Ligands
Triazines
Plasma (human)
Biomarkers
Adsorbents
Purification
Recovery
Pharmaceutical Preparations
Proteins

Keywords

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

Cite this

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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.",
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AU - Figueiredo, Carina

AU - Viecinski, Aline Canani

AU - Pina, Ana Sofia

AU - Barbosa, Arménio J. M.

AU - Roque, A. Cecília A.

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AB - 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.

KW - Affinity ligands

KW - Combinatorial chemistry

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KW - Protein purification

KW - Synthetic ligands

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