## Abstract Bifunctional affinity ligands based on a triazine scaffold were rationally designed to target prion protein and shown to bind recombinant prion protein with high affinity and selectivity. The ligands were capable of discriminating between prion protein glycoforms and monomeric and dimer
Design and synthesis of affinity ligands and relation of their structure with adsorption of proteins
✍ Scribed by Long Ye; Aizhang Xu; Chao Cheng; Li Zhang; Chenxi Huo; Feiyun Huang; Hong Xu; Rongxiu Li
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 731 KB
- Volume
- 34
- Category
- Article
- ISSN
- 1615-9306
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✦ Synopsis
Abstract
Affinity chromatography has played an increasingly important role both in the pharmaceutical industry and academic research. In the present study, we report our preliminary investigation on the relationship between the affinity ligand structure and its adsorption to multi‐protein samples. The structure of the ligands, including the size of the ring (cyclic group) and the length of the chain (linear group), has a great impact on the adsorption of ligands to proteins. Meanwhile, the functional groups that the ligands carry are also closely related to the adsorption of ligands to proteins. This research provides good guidance for the design and synthesis of affinity materials in affinity chromatography. It is also useful to other protein–ligand interaction‐related research.
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