{"title":"A Thioether-Bridging Surface Modification of Polymeric Microspheres Offers Nonbiological Protein A-Mimetic Affinity for IgG","authors":"Takanori Kishida","doi":"10.1002/admi.202301028","DOIUrl":null,"url":null,"abstract":"<p>Surface modification of polymeric materials to control their interaction with proteins has been studied extensively, leading to widespread bio-applications. However, the development of nonbiological, smart polymer surfaces, mimicking the recognition ability of biomolecules, remains a challenge. The present study presents a thioether-bridging surface modification of polymeric microspheres as a new approach for mimicking protein A affinity for immunoglobulin G (IgG). The bridge-modified surface is created through an epoxide linking reaction of porous polymeric microspheres with potassium thioacetate in a 2:1 molar ratio, acting as a protein A ligand, which is essential for industrial IgG purification. This surface exhibits buffer responsiveness and selective high-affinity binding to the IgG Fc region. Remarkably, a comparison among the binding behaviors of a series of thioether-modified microspheres indicates that bridging structures composed of β,β′-dihydroxysulfide play a predominant role in IgG recognition. This straightforward approach can lead to the development of economical and practical nonbiological alternatives to protein A-conjugated materials, providing solutions for various applications such as biosensors and site-specific reagents utilizing the affinity of the IgG Fc region. The improved understanding of protein interactions at bridged/non-bridged interfaces can be valuable in various applications such as implant materials and biomaterials.</p>","PeriodicalId":115,"journal":{"name":"Advanced Materials Interfaces","volume":null,"pages":null},"PeriodicalIF":4.3000,"publicationDate":"2024-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/admi.202301028","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advanced Materials Interfaces","FirstCategoryId":"88","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/admi.202301028","RegionNum":3,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
Abstract
Surface modification of polymeric materials to control their interaction with proteins has been studied extensively, leading to widespread bio-applications. However, the development of nonbiological, smart polymer surfaces, mimicking the recognition ability of biomolecules, remains a challenge. The present study presents a thioether-bridging surface modification of polymeric microspheres as a new approach for mimicking protein A affinity for immunoglobulin G (IgG). The bridge-modified surface is created through an epoxide linking reaction of porous polymeric microspheres with potassium thioacetate in a 2:1 molar ratio, acting as a protein A ligand, which is essential for industrial IgG purification. This surface exhibits buffer responsiveness and selective high-affinity binding to the IgG Fc region. Remarkably, a comparison among the binding behaviors of a series of thioether-modified microspheres indicates that bridging structures composed of β,β′-dihydroxysulfide play a predominant role in IgG recognition. This straightforward approach can lead to the development of economical and practical nonbiological alternatives to protein A-conjugated materials, providing solutions for various applications such as biosensors and site-specific reagents utilizing the affinity of the IgG Fc region. The improved understanding of protein interactions at bridged/non-bridged interfaces can be valuable in various applications such as implant materials and biomaterials.
为控制聚合物材料与蛋白质的相互作用而对其进行表面改性的研究已十分广泛,并已在生物领域得到广泛应用。然而,开发模仿生物分子识别能力的非生物智能聚合物表面仍然是一项挑战。本研究提出了一种硫醚桥接聚合物微球表面改性的新方法,用于模拟蛋白 A 对免疫球蛋白 G (IgG) 的亲和力。桥接改性表面是通过多孔聚合物微球与硫代乙酸钾以 2:1 的摩尔比进行环氧化物连接反应而产生的,硫代乙酸钾可作为蛋白 A 的配体,而蛋白 A 是工业 IgG 纯化所必需的。这种表面具有缓冲响应性,可选择性地与 IgG Fc 区域高亲和性结合。值得注意的是,对一系列硫醚修饰微球的结合行为进行比较后发现,由 β,β′-二羟基硫醚组成的桥接结构在 IgG 识别中起着主导作用。这种直接的方法可以开发出经济实用的非生物替代品,替代蛋白 A 结合材料,为生物传感器和利用 IgG Fc 区域亲和力的位点特异性试剂等各种应用提供解决方案。加深对桥接/非桥接界面上蛋白质相互作用的了解,对植入材料和生物材料等各种应用都很有价值。
期刊介绍:
Advanced Materials Interfaces publishes top-level research on interface technologies and effects. Considering any interface formed between solids, liquids, and gases, the journal ensures an interdisciplinary blend of physics, chemistry, materials science, and life sciences. Advanced Materials Interfaces was launched in 2014 and received an Impact Factor of 4.834 in 2018.
The scope of Advanced Materials Interfaces is dedicated to interfaces and surfaces that play an essential role in virtually all materials and devices. Physics, chemistry, materials science and life sciences blend to encourage new, cross-pollinating ideas, which will drive forward our understanding of the processes at the interface.
Advanced Materials Interfaces covers all topics in interface-related research:
Oil / water separation,
Applications of nanostructured materials,
2D materials and heterostructures,
Surfaces and interfaces in organic electronic devices,
Catalysis and membranes,
Self-assembly and nanopatterned surfaces,
Composite and coating materials,
Biointerfaces for technical and medical applications.
Advanced Materials Interfaces provides a forum for topics on surface and interface science with a wide choice of formats: Reviews, Full Papers, and Communications, as well as Progress Reports and Research News.