Fig 1: Micrographs (40x) of immunofluorescence staining for PD-L1 in (a) C6 cells, demonstrating negative PD-L1 expression, (b) HC116 cells (PD-L1 positive), and (c) HCC827 cells (PD-L1 positive); (merged images: cell nuclei stained in blue with DAPI and PD-L1 stained in green with anti-PD-L1). (d) Cellular uptake and (e) internalization of [99mTc]Tc-WL12, [99mTc]Tc-iPD-L1, and 99mTcO4−in C6, HCT116, and HCC827 cells. Two-way ANOVA statistical analysis (alpha 0.05) showed that there were significant differences (p < 0.0001) in the percentage of uptake and internalization due to both the cell type factor (C6, HCT116, and HCC827) and the radiotracer type ([99mTc]Tc-WL12, [99mTc]Tc-iPD-L1, and 99mTcO4−).
Fig 2: The WL12 ligand has the hydrogen atom as a substituent of the R1 group (Figure 1). The image on the left shows the docking of the WL12 ligand with the PD-L1 protein, interacting with the residues described in Table 1. The right side shows the intermolecular interactions between the ligand and the PD-L1 receptor, and the distances are shown in Å scale.
Fig 3: The HYNIC-WL12 ligand has the HYNIC molecule as a substituent of the R1 group (Figure 1). The image on the left shows the docking of the HYNIC-WL12 ligand with the PD-L1 protein, interacting with the residues described in Table 1. The right side shows the intermolecular interactions between the ligand and the PD-L1 receptor.
Fig 4: SDS-PAGE (radio-SDS-PAGE). Migration of [99mTc]Tc-iPD-L1 (Rf = 0.6–0.7; 60–70 mm) and [99mTc]Tc-WL12 (Rf = 0.6–0.7; 60–70 mm). (a) Interaction [99mTc]Tc-WL12-PDL1 protein showing 14% of the radioactivity shifted at a distance associated with the PD-L1 protein. (b) Interaction [99mTc]Tc-iPD-L1-PDL1 protein showing 30% of the radioactivity shifted at a distance associated with the PD-L1 protein. (c,d) No shift in radioactivity when [99mTc]Tc-WL12-PDL1 and [99mTc]Tc-iPD-L1-PDL1 interact with the integrin protein (negative control). (e) Migration of PD-L1 (Rf = 0.4; 40 mm) and integrin (Rf = 0.0; 0.0 mm) in the gel plate.
Fig 5: The iPD-L1 ligand has the HYNIC molecule as a substituent of the R1 group (Figure 1). The image on the left shows the docking of the iPD-L1 ligand with the PD-L1 protein, interacting with the residues described in Table 1. The right side shows the intermolecular interactions between the ligand and the PD-L1 receptor, and the distances are shown in Å scale.
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