Designed affinity ligands to capture human serum albumin

Raquel dos Santos; Carina Figueiredo; Aline Canani Viecinski; Ana Sofia Pina; Arménio J. M. Barbosa; A. Cecília A. Roque

doi:10.1016/j.chroma.2018.11.021

Designed affinity ligands to capture human serum albumin

Raquel dos Santos, Carina Figueiredo, Aline Canani Viecinski, Ana Sofia Pina, Arménio J. M. Barbosa, A. Cecília A. Roque

Research output: Contribution to journal › Article › peer-review

16 Citations (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 language	English
Pages (from-to)	88-97
Journal	Journal Of Chromatography A
Volume	1583
DOIs	https://doi.org/10.1016/j.chroma.2018.11.021
Publication status	Published - 4 Jan 2019

Keywords

Affinity ligands
Combinatorial chemistry
Human serum albumin
Protein purification
Synthetic ligands

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.chroma.2018.11.021Licence: CC BY-NC-ND

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title = "Designed affinity ligands to capture human serum albumin",

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

KW - Human serum albumin

KW - Protein purification

KW - Synthetic ligands

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JF - Journal Of Chromatography A

ER -

Designed affinity ligands to capture human serum albumin

Abstract

Keywords

UN SDGs

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