Developing an antibody-binding protein cage as a molecular recognition drug modular nanoplatform

Kang, Hyo Jin; Kang, Young Ji; Lee, Young-Mi; Shin, Hong Ju; Chung, Sang J.; Kang, Sebyung

doi:10.1016/j.biomaterials.2012.03.055

Cited by 65 publications

(78 citation statements)

References 40 publications

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“…In addition we developed an Fc-III functionalized protein nanocage (bound to anti-Her2 Ab called trastuzumab or Herceptin) to specifically target breast cancer cells (Figure 6) [71,72]. Breast cancer cells are known to overexpress Her2 receptors on the cell surface.…”

Section: Modern Applications Of Immunoglobulin Binding Ligandsmentioning

confidence: 99%

Fc-Binding Ligands of Immunoglobulin G: An Overview of High Affinity Proteins and Peptides

2016

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The rapidly increasing application of antibodies has inspired the development of several novel methods to isolate and target antibodies using smart biomaterials that mimic the binding of Fc-receptors to antibodies. The Fc-binding domain of antibodies is the primary binding site for e.g., effector proteins and secondary antibodies, whereas antigens bind to the Fab region. Protein A, G, and L, surface proteins expressed by pathogenic bacteria, are well known to bind immunoglobulin and have been widely exploited in antibody purification strategies. Several difficulties are encountered when bacterial proteins are used in antibody research and application. One of the major obstacles hampering the use of bacterial proteins is sample contamination with trace amounts of these proteins, which can invoke an immune response in the host. Many research groups actively develop synthetic ligands that are able to selectively and strongly bind to antibodies. Among the reported ligands, peptides that bind to the Fc-domain of antibodies are attractive tools in antibody research. Besides their use as high affinity ligands in antibody purification chromatography, Fc-binding peptides are applied e.g., to localize antibodies on nanomaterials and to increase the half-life of proteins in serum. In this review, recent developments of Fc-binding peptides are presented and their binding characteristics and diverse applications are discussed.

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Section: Modern Applications Of Immunoglobulin Binding Ligandsmentioning

confidence: 99%

Fc-Binding Ligands of Immunoglobulin G: An Overview of High Affinity Proteins and Peptides

2016

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“…SPR은 펩타이드-항체 반응, 단백질-항체 반응, 단백질-DNA 반응, 단백질-다당류 반응, 단백질-바이러스 반응, DNA-DNA 반응 연구에 사용되고 있다. 이와 같이 SPR을 이용한 측정 이 바이오 연구에서 광범위하게 시용되면서 미량 생체물질 의 측정을 위하여 SPR의 측정 감도를 향상시키려는 연구가 활발하게 진행되고 있다 [4][5][6] . 그러나 기존 SPR 측정법은 금이나 은 등의 금속박막을 사 용하고 있으며 금속박막은 제작 방법이나 표면 상태에 따라 측정감도가 바뀌고 균질성이 없어 신뢰성 있는 측정 장비로 사용하는데 문제점을 안고 있다.…”

Section: 서 론unclassified

Measurement and Analysis of the Dynamics of Peptide-Antibody Interactions Using an Ellipsometric Biosensor Based on a Silicon Substrate

이근재¹,

Cho²,

Heung³

2017

Korean Journal of Optics and Photonics

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We precisely measured and analyzed the dynamics of peptide-antibody interactions, using an ellipsometric biosensor based on a silicon substrate. To reduce the signal error due to the imperfect flatness of the substrate for extremely low concentrations of peptide, we fabricated the biosensor with a silicon substrate coated with Dextran SAM, instead of a glass prism coated with a thin metallic thin film. At an injection speed of 100 µl/min of buffer liquid, we detected the dynamics of antibody-Dextran SAM or peptide-antibody fixed on biosensor, respectively. We detected the dynamics of antibody-Dextran SAM interactions down to a low concentration of 5 ng per liter, and we precisely measured the dynamics of association and dissociation of peptide and antibody down to 100 nM of peptide. We obtained the rate constants for association and dissociation from fitting the data by using deduced dynamical equation. As a result, we obtained an equilibrium constant for dissociation of 97 nM of peptide-antibody complex, which belongs to Class I.

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“…23 Briefly, 0.5 mg/mL of AFn was dissolved in 0.15 M NaCl. Then, DOX was added into the solution at a final concentration of 1 mg/mL and gently stirred …”

Section: Preparation Of Dox-loaded Afnmentioning

confidence: 99%

Construction of magnetic-carbon-quantum-dots-probe-labeled apoferritin nanocages for bioimaging and targeted therapy

Yao¹,

Su²,

Zeng³

et al. 2016

IJN

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Carbon dots (CDs) are one of the most highlighted carbon-based materials for biological applications, such as optical imaging nanoprobes, which are used for labeling cells in cancer treatment mainly due to their biocompatibility and unique optical properties. In this study, gadolinium (Gd)-complex-containing CDs were obtained through a one-step microwave method to develop multimodal nanoprobes integrating the advantages of optical and magnetic imaging. The obtained Gd-CDs exhibited highly fluorescent properties with excellent water solubility and biological compatibility. Natural apoferritin (AFn) nanocages, an excellent drug delivery carrier, are hollow in structure, with their pH-dependent, unfolding–refolding process at pH 2.0 and 7.4. The chemotherapeutic drug doxorubicin (DOX) can be highly effective and encapsulated into AFn cavity. A widely used tumor-targeting molecule, folic acid (FA), functionalized the surface of AFn to obtain an active tumor targeting effect on MCF-7 cells and malignant tumors in mice models. In this study, an AFn nanocarrier encapsulating high concentration of DOX labeled with magnetic and fluorescent Gd-CDs probe was developed. Gd-CDs exhibited a unique green photoluminescence and almost no toxicity compared with free GdCl 3 . Furthermore, Gd-doped CDs significantly increased the circulation time and decreased the toxicity of Gd 3+ in in vitro and in vivo magnetic resonance imaging, which demonstrated that the AFn nanocages labeled with Gd-CD compounds could serve as an excellent T 1 contrast agent for magnetic resonance imaging. The self-assembling multifunctional Gd-CDs/AFn (DOX)/FA nanoparticles have a great potential for cancer theranostic applications.

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Developing an antibody-binding protein cage as a molecular recognition drug modular nanoplatform

Cited by 65 publications

References 40 publications

Fc-Binding Ligands of Immunoglobulin G: An Overview of High Affinity Proteins and Peptides

Fc-Binding Ligands of Immunoglobulin G: An Overview of High Affinity Proteins and Peptides

Measurement and Analysis of the Dynamics of Peptide-Antibody Interactions Using an Ellipsometric Biosensor Based on a Silicon Substrate

Construction of magnetic-carbon-quantum-dots-probe-labeled apoferritin nanocages for bioimaging and targeted therapy

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