2020
DOI: 10.1186/s13550-020-00694-2
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[68Ga]ABY-028: an albumin-binding domain (ABD) protein-based imaging tracer for positron emission tomography (PET) studies of altered vascular permeability and predictions of albumin-drug conjugate transport

Abstract: Background Albumin is commonly used as a carrier platform for drugs to extend their circulatory half-lives and influence their uptake into tissues that have altered permeability to the plasma protein. The albumin-binding domain (ABD) protein, which binds in vivo to serum albumin with high affinity, has proven to be a versatile scaffold for engineering biopharmaceuticals with a range of binding capabilities. In this study, the ABD protein equipped with a mal-DOTA chelator (denoted ABY-028) was radiolabeled with… Show more

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Cited by 9 publications
(4 citation statements)
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“…This was in line with previously published data on puri cation strategy for crude radiotracers based on A body molecules. (12,19) It was discovered that approximately 50% of the ABY-025 peptide was lost from addition in the reaction vial to what was present in the nal product (compare the 0.9 mg addition in the reaction vial to the chemical concentration of ABY-025 presented in Table 7). Aiming for a nal product containing approximately 0.5 mg of peptide, adding 0.9 mg of peptide into the reaction vial was found suitable.…”
Section: Resultsmentioning
confidence: 99%
“…This was in line with previously published data on puri cation strategy for crude radiotracers based on A body molecules. (12,19) It was discovered that approximately 50% of the ABY-025 peptide was lost from addition in the reaction vial to what was present in the nal product (compare the 0.9 mg addition in the reaction vial to the chemical concentration of ABY-025 presented in Table 7). Aiming for a nal product containing approximately 0.5 mg of peptide, adding 0.9 mg of peptide into the reaction vial was found suitable.…”
Section: Resultsmentioning
confidence: 99%
“…10 Several radiolabeled molecules and peptides have been reported for versatile imaging purposes, such as [ 18 F]AlF-NEB, 13 [ 64 Cu]Cu-NEB, 13 [ 68 Ga]Ga-NEB, 14 [ 131 I]IBA, 15 and [ 68 Ga]Ga-ABY-028. 27 They bind to serum albumins in vivo non-covalently with nanomolar (K d = 3.4 nM for [ 68 Ga]Ga-ABY-028) to micromolar (IC 50 = 46.5 μM for [ 131 I]IBA) binding affinities. For blood pool imaging, [ 68 Ga]Ga-DM was comparable to [ 68 Ga]Ga-NEB at 1 h p.i.…”
Section: ■ Discussionmentioning
confidence: 99%
“…Studies on healthy rats have shown that [ 68 Ga]ABY-028, an albumin-binding domain protein-based imaging tracer for positron emission tomography, binds in vivo to albumin, acquires albumin circulatory behavior, and accumulates in liver, spleen, and in muscle tissues [ 75 ]. Similar data were published by Park and collaborators [ 76 ] who noticed effective accumulation of 64 [Cu]-labeled-click chemistry-based albumin nanoplatform conjugates in normal lung, liver, kidney, intestine, and heart with an over four-fold higher uptake than the tumor at 1 h post-injection.…”
Section: Diffusion and Abp-mediated Mechanisms Could Underlie The Accumulation Of Rtkis Bound To Albumin In Healthy Organs And Tissuesmentioning
confidence: 99%