scholarly journals Copper-64-Labeled Antibody Fragments for Immuno-PET/Radioimmunotherapy with Low Renal Radioactivity Levels and Amplified Tumor-Kidney Ratios

ACS Omega ◽  
2021 ◽  
Author(s):  
Hiroyuki Suzuki ◽  
Shota Kise ◽  
Yuta Kaizuka ◽  
Reo Watanabe ◽  
Tsubasa Sugawa ◽  
...  
Keyword(s):  
Antibody Fragments ◽  
Radioactivity Levels

Design, Synthesis, and Evaluation of [188Re]Organorhenium-Labeled Antibody Fragments with Renal Enzyme-Cleavable Linkage for Low Renal Radioactivity Levels

2007 ◽  
Vol 18 (1) ◽  
pp. 190-198 ◽  
Author(s):  
Tomoya Uehara ◽  
Miho Koike ◽  
Hideo Nakata ◽  
Hiroshi Hanaoka ◽  
Yasuhiko Iida ◽  
...  
Keyword(s):  
Antibody Fragments ◽  
Design Synthesis ◽  
Radioactivity Levels

In Vitro System To Estimate Renal Brush Border Enzyme-Mediated Cleavage of Peptide Linkages for Designing Radiolabeled Antibody Fragments of Low Renal Radioactivity Levels

2005 ◽  
Vol 16 (6) ◽  
pp. 1610-1616 ◽  
Author(s):  
Yasushi Fujioka ◽  
Satoshi Satake ◽  
Tomoya Uehara ◽  
Takahiro Mukai ◽  
Hiromichi Akizawa ◽  
...  
Keyword(s):  
Brush Border ◽  
Antibody Fragments ◽  
In Vitro System ◽  
Brush Border Enzyme ◽  
Renal Brush Border ◽  
Radioactivity Levels

Renal Brush Border Enzyme-Cleavable Linkages for Low Renal Radioactivity Levels of Radiolabeled Antibody Fragments

2013 ◽  
Vol 24 (2) ◽  
pp. 291-299 ◽  
Author(s):  
Hiromichi Akizawa ◽  
Mitsuo Imajima ◽  
Hirofumi Hanaoka ◽  
Tomoya Uehara ◽  
Satoshi Satake ◽  
...  
Keyword(s):  
Brush Border ◽  
Antibody Fragments ◽  
Brush Border Enzyme ◽  
Renal Brush Border ◽  
Radioactivity Levels

Specific Labeling of Protein Domains with Antibody Fragments

1981 ◽  
Vol 39 ◽  
pp. 416-417
Author(s):  
U. Aebi ◽  
L.E. Buhle ◽  
W.E. Fowler
Keyword(s):  
Image Processing ◽  
Specific Protein ◽  
Antibody Fragments ◽  
Supramolecular Organization ◽  
Two Dimensional ◽  
Ordered Structures ◽  
Virus Capsids ◽  
Processing Techniques

Many important supramolecular structures such as filaments, microtubules, virus capsids and certain membrane proteins and bacterial cell walls exist as ordered polymers or two-dimensional crystalline arrays in vivo. In several instances it has been possible to induce soluble proteins to form ordered polymers or two-dimensional crystalline arrays in vitro. In both cases a combination of electron microscopy of negatively stained specimens with analog or digital image processing techniques has proven extremely useful for elucidating the molecular and supramolecular organization of the constituent proteins. However from the reconstructed stain exclusion patterns it is often difficult to identify distinct stain excluding regions with specific protein subunits. To this end it has been demonstrated that in some cases this ambiguity can be resolved by a combination of stoichiometric labeling of the ordered structures with subunit-specific antibody fragments (e.g. Fab) and image processing of the electron micrographs recorded from labeled and unlabeled structures.

Evaluation of 99mTc-Label led Vitamin K4 as an Agent for Testicular Imaging

1991 ◽  
Vol 30 (01) ◽  
pp. 35-39 ◽  
Author(s):  
H. S. Durak ◽  
M. Kitapgi ◽  
B. E. Caner ◽  
R. Senekowitsch ◽  
M. T. Ercan
Keyword(s):  
Soft Tissue ◽  
Room Temperature ◽  
Normal Subjects ◽  
Left Testis ◽  
Wide Range ◽  
Activity Ratios ◽  
The Right ◽  
Radioactivity Levels

Vitamin K4 was labelled with 99mTc with an efficiency higher than 97%. The compound was stable up to 24 h at room temperature, and its biodistribution in NMRI mice indicated its in vivo stability. Blood radioactivity levels were high over a wide range. 10% of the injected activity remained in blood after 24 h. Excretion was mostly via kidneys. Only the liver and kidneys concentrated appreciable amounts of radioactivity. Testis/soft tissue ratios were 1.4 and 1.57 at 6 and 24 h, respectively. Testis/blood ratios were lower than 1. In vitro studies with mouse blood indicated that 33.9 ±9.6% of the radioactivity was associated with RBCs; it was washed out almost completely with saline. Protein binding was 28.7 ±6.3% as determined by TCA precipitation. Blood clearance of 99mTc-l<4 in normal subjects showed a slow decrease of radioactivity, reaching a plateau after 16 h at 20% of the injected activity. In scintigraphic images in men the testes could be well visualized. The right/left testis ratio was 1.08 ±0.13. Testis/soft tissue and testis/blood activity ratios were highest at 3 h. These ratios were higher than those obtained with pertechnetate at 20 min post injection.99mTc-l<4 appears to be a promising radiopharmaceutical for the scintigraphic visualization of testes.

SOME EFFECTS OF PERCHLORATE ON THE DISTRIBUTION OF 131-IODIDE

1965 ◽  
Vol 50 (2) ◽  
pp. 195-201 ◽  
Author(s):  
E. Schönbaum ◽  
E. A. Sellers ◽  
M.J. Gill
Keyword(s):  
Urinary Excretion ◽  
Renal Excretion ◽  
Kidney Tissue ◽  
Intraperitoneal Dose ◽  
Blood Radioactivity ◽  
Radioactivity Levels

ABSTRACT The distribution of an intraperitoneal dose of 131-iodide was studied in rats receiving perchlorate. The accumulation of radioactivity in the stomach, which occurred soon after injection in controls, was inhibited by perchlorate. Concurrent with this, radioactivity in blood was higher in perchlorate treated rats than in controls. After perchlorate, more radioactivity in kidney tissue and an elevated urinary excretion of the tracer was noted. After 24 hours, plasma radioactivity was lower in perchlorate treated rats than in controls. Increased renal excretion of 131I after perchlorate is, at least in part, due to higher blood radioactivity levels, probably because of decreased iodide space due to the action of perchlorate.

A Plug-and-Play Approach for the De Novo Generation of Dually Functionalised Bispecifics

2019 ◽  
Author(s):  
Antoine Maruani ◽  
Peter A. Szijj ◽  
Calise Bahou ◽  
João C. F. Nogueira ◽  
Stephen Caddick ◽  
...  
Keyword(s):  
De Novo ◽  
Therapeutic Index ◽  
Antibody Fragments ◽  
Bispecific Antibodies ◽  
Full Potential ◽  
Mechanisms Of Resistance ◽  
Large Excess ◽  
Chemical Methods ◽  
New Class ◽  
Novel Approach

<p>Diseases are multifactorial, with redundancies and synergies between various pathways. However, most of the antibody-based therapeutics in clinical trials and on the market interact with only one target thus limiting their efficacy. The targeting of multiple epitopes could improve the therapeutic index of treatment and counteract mechanisms of resistance. To this effect, a new class of therapeutics emerged: bispecific antibodies.</p><p>Bispecific formation using chemical methods is rare and low yielding and/or requires a large excess of one of the two proteins to avoid homodimerisation. In order for chemically prepared bispecifics to deliver their full potential, high-yielding, modular and reliable cross-linking technologies are required. Herein, we describe a novel approach not only for the rapid and high-yielding chemical generation of bispecific antibodies from native antibody fragments, but also for the site-specific dual functionalisation of the resulting bioconjugates. Based on orthogonal clickable functional groups, this strategy enables the assembly of functionalised bispecifics with controlled loading in a modular and convergent manner.</p>

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