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A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)
A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)
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A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)
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A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)
A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)

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A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)
A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)
Journal Article

A Thioether‐Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A‐Mimetic Affinity for IgG (Adv. Mater. Interfaces 23/2024)

2024
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Overview
Bridging Surface Modification Just like the kids spreading their nets in pairs, thioether‐bridge‐modified polymeric surfaces selectively capture immunoglobulin G (IgG). Furthermore, they exhibit buffer responsiveness and high‐affinity binding to the IgG Fc region, acting as protein A ligands. The bridging surface modification approach and the improved understanding of protein interactions at bridged/non‐bridged interfaces could be valuable in widespread bio‐applications. More details can be found in the article 2301028 by Takanori Kishida.