Trastuzumab-modified nanoparticles: Optimisation of preparation and uptake in cancer cells

Steinhauser, I; Spänkuch, Birgit; Strebhardt, Klaus; Langer, Klaus

doi:10.1016/j.biomaterials.2006.05.016

Cited by 197 publications

(129 citation statements)

References 24 publications

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“…Trastuzumab is a humanized Ab directed against human epidermal growth factor receptor 2 (HER2), which is expressed in some types of breast cancer cells. It has been reported that trastuzumab is taken up by HER2-expressing cells via HER2-mediated endocytosis (39,40). Rituximab, a chimeric Ab directed against CD20, is also internalized in an Ag-mediated manner (41).…”

Section: Discussionmentioning

confidence: 99%

Importance of Neonatal FcR in Regulating the Serum Half-Life of Therapeutic Proteins Containing the Fc Domain of Human IgG1: A Comparative Study of the Affinity of Monoclonal Antibodies and Fc-Fusion Proteins to Human Neonatal FcR

Suzuki

Ishii‐Watabe

Tada

et al. 2010

The Journal of Immunology

308

239

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The neonatal FcR (FcRn) binds to the Fc domain of IgG at acidic pH in the endosome and protects IgG from degradation, thereby contributing to the long serum half-life of IgG. To date, more than 20 mAb products and 5 Fc-fusion protein products have received marketing authorization approval in the United States, the European Union, or Japan. Many of these therapeutic proteins have the Fc domain of human IgG1; however, the serum half-lives differ in each protein. To elucidate the role of FcRn in the pharmacokinetics of Fc domain-containing therapeutic proteins, we evaluated the affinity of the clinically used human, humanized, chimeric, or mouse mAbs and Fc-fusion proteins to recombinant human FcRn by surface plasmon resonance analysis. The affinities of these therapeutic proteins to FcRn were found to be closely correlated with the serum half-lives reported from clinical studies, suggesting the important role of FcRn in regulating their serum half-lives. The relatively short serum half-life of Fc-fusion proteins was thought to arise from the low affinity to FcRn. The existence of some mAbs having high affinity to FcRn and a short serum half-life, however, suggested the involvement of other critical factor(s) in determining the serum half-life of such Abs. We further investigated the reason for the relatively low affinity of Fc-fusion proteins to FcRn and suggested the possibility that the receptor domain of Fc-fusion protein influences the structural environment of the FcRn binding region but not of the FcγRI binding region of the Fc domain.

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Section: Discussionmentioning

confidence: 99%

Importance of Neonatal FcR in Regulating the Serum Half-Life of Therapeutic Proteins Containing the Fc Domain of Human IgG1: A Comparative Study of the Affinity of Monoclonal Antibodies and Fc-Fusion Proteins to Human Neonatal FcR

Suzuki

Ishii‐Watabe

Tada

et al. 2010

The Journal of Immunology

308

239

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“…Thus, this system provides the basis for tumor-targeted drug delivery with the potential to minimize the side effects caused by nonspecific internalization by healthy tissues. [34] Importantly, since coupling of the antibody to the nanoparticle was undertaken only at sites where the disulfide groups were reduced prior to coupling, a degree of site specificity could be introduced into the protein-coupling reaction. This is not possible using amide formation (since free amine groups are generally widely spaced within the antibody structure).…”

Section: Disulfide Functional Groups/maleimide-thiol Couplingmentioning

confidence: 99%

Recent Advances in the Generation of Antibody–Nanomaterial Conjugates

Sivaram

Wardiana

Howard

et al. 2017

Adv Healthcare Materials

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Targeted nanomedicines have significantly changed the way new therapeutics are designed to treat disease. Central to successful therapeutics is the ability to control the dynamics of protein–nanomaterial interactions to enhance the therapeutic effect of the nanomedicine. The aim of this review is to illustrate the diversity and versatility of the conjugation approaches involved in the synthesis of antibody–nanoparticle conjugates, and highlight significant new advances in the field of bioconjugation. Such nanomedicines have found utility as both advanced therapeutic agents, as well as more complex imaging contrast agents that can provide both anatomical and functional information of diseased tissue. While such conjugates show significant promise as next generation targeted nanomedicines, it is recognized that there are in fact no clinically approved targeted therapeutics on the market. This fact is reflected upon within this review, and attempts are made to draw some reasoning from the complexities associated with the bioconjugation chemistry approaches that are typically utilized. Present trends, as well as future directions of next generation targeted nanomedicines are also discussed.

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“…Nanoparticle systems conjugated with HER-2 antibody fragment are being investigated for selective imaging, drug delivery and gene silencing through siRNA [50,51]. As in the case of prostate cancer, folate-receptor-mediated nanoparticle systems are also being developed.…”

Section: Breast Cancer Selectionmentioning

confidence: 99%

The potential legacy of cancer nanotechnology: cellular selection

Patra

Turner

2014

Trends in Biotechnology

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Overexpression of oncogenes or loss of tumour suppressors can transform a normal cell to a cancerous one, resulting in uncontrolled regulation of intracellular signaling pathways and immunity to stresses, which both pose therapeutic challenges.Conventional approaches to cancer therapy, although they are effective at killing cancer cells, may still fail due to inadequate biodistribution and unwanted side effects.Nanotechnology-based approaches provide a promising alternative, with the possibility of targeting cells at an early stage, during their transformation into cancer cells. This review considers techniques that specifically target those molecular changes, which begin in only a very small percentage of normal cells as they undergo transformation. These techniques are crucial for 'early-stage' diagnosis and therapy.3

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Trastuzumab-modified nanoparticles: Optimisation of preparation and uptake in cancer cells

Cited by 197 publications

References 24 publications

Importance of Neonatal FcR in Regulating the Serum Half-Life of Therapeutic Proteins Containing the Fc Domain of Human IgG1: A Comparative Study of the Affinity of Monoclonal Antibodies and Fc-Fusion Proteins to Human Neonatal FcR

Importance of Neonatal FcR in Regulating the Serum Half-Life of Therapeutic Proteins Containing the Fc Domain of Human IgG1: A Comparative Study of the Affinity of Monoclonal Antibodies and Fc-Fusion Proteins to Human Neonatal FcR

Recent Advances in the Generation of Antibody–Nanomaterial Conjugates

The potential legacy of cancer nanotechnology: cellular selection

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