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Tumor imaging using a picomolar affinity HER2 binding affibody molecule.
TLDR
A HER2-specific 6 kDa Affibody molecule with 22 pmol/L affinity that can be used for the visualization of HER2 expression in tumors in vivo using gamma camera is described and shows clear, high-contrast visualization of Her2-expressing xenografts in mice as early as 6 hours post-injection. Expand
Selection and characterization of HER2/neu-binding affibody ligands.
TLDR
Two affibody variants were shown to selectively bind to the extracellular domain of HER2/neu (HER2-ECD), but not to control proteins, which might be considered in tumor targeting applications for radionuclide diagnostics and therapy of adenocarcinomas such as breast and ovarian cancers. Expand
Affibody molecules: Engineered proteins for therapeutic, diagnostic and biotechnological applications
TLDR
Cumulative evidence suggests that the three helical scaffold domain used as basis for these molecules is highly suited to create a molecular affinity handle for vastly different applications. Expand
Radionuclide therapy of HER2-positive microxenografts using a 177Lu-labeled HER2-specific Affibody molecule.
TLDR
It is reported that reversible binding to albumin efficiently reduces the renal excretion and uptake, enabling radiometal-based nuclide therapy and improving the in vivo biodistribution. Expand
Molecular Imaging of HER2-Expressing Malignant Tumors in Breast Cancer Patients Using Synthetic 111In- or 68Ga-Labeled Affibody Molecules
TLDR
Molecular imaging using 111In- or 68Ga-labeled ABY-002 has the potential to localize metastatic lesions in vivo, adds qualitative information not available today by conventional imaging techniques, and may allow the HER2 status to be determined for metastases not amenable to biopsy. Expand
Design of an optimized scaffold for affibody molecules.
TLDR
The optimized scaffold contains 11 amino acid substitutions in the nonbinding surface and is characterized by improved thermal and chemical stability, as well as increased hydrophilicity, and enables generation of identical Affibody molecules both by chemical peptide synthesis and by recombinant bacterial expression. Expand
Directed evolution to low nanomolar affinity of a tumor-targeting epidermal growth factor receptor-binding affibody molecule.
TLDR
The affinity maturation procedure for the generation of Affibody molecules binding with high affinity and specificity to epidermal growth factor receptor 1 is described. Expand
Pharmacokinetics and red cell utilization of 52Fe/59Fe‐labelled iron polymaltose in anaemic patients using positron emission tomography
TLDR
High red cell utilization of iron polymaltose occurred in anaemic patients and the reticuloendothelial uptake of this complex may reflect the safety of polysaccharide complexes. Expand
Comparative in vivo evaluation of technetium and iodine labels on an anti-HER2 affibody for single-photon imaging of HER2 expression in tumors.
TLDR
A stable, site-specifically labeled 99mTc-His6-(ZHER2:4)2 conjugate was prepared that was able to bind to HER2-expressing cells in vitro and in vivo and was much more favorable for the radioiodinated Affibody. Expand
Affibody Molecules for Epidermal Growth Factor Receptor Targeting In Vivo: Aspects of Dimerization and Labeling Chemistry
TLDR
The radiometal-labeled monomeric Affibody molecule ZEGFR:1907 has a potential for radionuclide molecular imaging of EGFR expression in malignant tumors and demonstrates superior cellular retention of radioactivity in tumors. Expand
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