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Nanobodies were derived from heavy-chain-only antibodies, raised in immunized dromedaries. Binding characteristics were evaluated through ELISA and flow cytometry. Selected nanobodies were radiolabeled with 99mTc at their hexahistidine tail, after which cell binding capacity and internalization were evaluated on PSMApos LNCaP and PSMAneg PC3 cell lines. In vivo tumor targeting was analyzed in both LNCaP and PC3 xenografted mice through SPECT/microCT and tissue sampling. A panel of 72 generated Ozagrel clones scored positive on ELISA, all contributing to three nanobody groups, of which group 3 dominated with 70 clones. ELISA and FACS analysis led to the selection of two dominant nanobodies. 99mTc-labeled PSMA6 and PSMA30 both showed specific binding on LNCAP cells, but not on PC3 cells. 99mTc-PSMA30 internalized significantly more in LNCaP cells compared to 99mTc-PSMA6. Higher absolute tumor uptake and tumor-to-normal organ ratios were observed for 99mTc-PSMA30 compared with 99mTc-PSMA6 find more and a 99mTc-control nanobody in LNCaP but not in PC3 tumor-bearing mice. PSMA30 nanobody has improved targeting characteristics both in vitro as well as in vivo compared with PSMA6 and the control nanobody, and was therefore selected as our in-house-developed lead compound for PSMA targeting. Copyright ? 2014 John Wiley & Sons, Ltd. ""63040" "Noninvasive detection of fibrin in vivo using diagnostic imaging modalities may improve clinical decision-making on possible therapeutic options in atherosclerosis, cancer and thrombus-related Selleck Galunisertib pathologies such as pulmonary embolism and deep venous thrombosis. The aim of this study was to assess the potential of a novel 111In-labeled fibrin-binding peptide (FibPep) to visualize thrombi in mice noninvasively using single-photon emission computed tomography (SPECT). FibPep and a negative control peptide (NCFibPep) were synthesized and their fibrin-binding properties were assessed in vitro. FibPep showed enhanced binding compared with NCFibPep to both fibrin and blood clots. FibPep bound to fibrin with a dissociation constant (Kd) of 0.8 �� m, whereas NCFibPep displayed at least a 100-fold lower affinity towards fibrin. A FeCl3-injury carotid artery thrombosis mouse model was used to evaluate the peptides in vivo. FibPep and NCFibPep displayed rapid blood clearance and were eliminated via the renal pathway. In vivo SPECT imaging using FibPep allowed clear visualization of thrombi. Ex vivo biodistribution showed significantly increased uptake of FibPep in the thrombus-containing carotid in comparison to the noninjured carotid (5.7?��?0.7 and 0.6?��?0.4% injected dose per gram (%ID g?1), respectively; p?