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. Author manuscript; available in PMC: 2020 Feb 21.
Published in final edited form as: Cell Chem Biol. 2018 Dec 6;26(2):213–222.e6. doi: 10.1016/j.chembiol.2018.10.019

Figure 3. Frozen pancreas sections offer a platform to visualize islet Zn2+ content and assess compound zinc chelation activity.

Figure 3.

(A) Fresh frozen INSCremTmG murine pancreatic section (10 μm thickness) expressing mTomato in INS− cells and GFP in INS+ cells stained with TSQ (10 μM). Islet area is outlined in yellow. (B) Structures of GNF-4877 (top left), the variable 4877 scaffold (top right), 4877-DPA, 4877-DBA, 4877-EXT-DPA, and 4877-EXT-DBA (bottom, from left) with either the chelating group dipicolylamine (DPA) appended or the non-chelating group dibenzylamine (DBA) appended. (C) Competition assay for Zn2+ binding with frozen sections treated sequentially with TSQ (10 μM) then vehicle, gatifloxacin (1 mM), CC-401 (1 mM), SAHA (1 mM), 4877-DBA (1 mM), GNF-4877 (1 mM), 4877-EXT-DBA (1 mM), TPEN (1 mM), oxytetracycline (1 mM), DPA (1 mM), 4877-DPA (1 mM) or 4877-EXT-DPA (0.5 mM). (D) Comparison of molecules’ zinc affinity on pancreas sections, characterized by IC50, Hill coefficient nH, and correlation coefficient R2. Data are represented as mean ± S.D.

See also Figure S3.