Dental Hygiene Laboratory, Coleman Bldg., Westbrook College, 1970s

Four Westbrook College dental hygiene students work in the dental hygiene laboratory in Coleman in this 1970s photograph by Ellis Herwig Photography of Cambridge, Mass.https://dune.une.edu/wchc_photos_labs/1028/thumbnail.jp

Additional file 2: of MASTL inhibition promotes mitotic catastrophe through PP2A activation to inhibit cancer growth and radioresistance in breast cancer cells

Figure S2. MASTL depletion increases G2 arrest and the accumulation of pH 3. a The quantification of the relative percentage of cells expressing red fluorescence (pH 3). b Representative images of a normal mitotic cells (left panel) and MASTL-depleted mitotic defect cells stained with anti-acetyl-tubulin antibody (green), anti-phospho-Histone H3 antibody (red), and DAPI (blue). Scale bar = 10 μm. (TIF 763 kb

Amphipathic α‑Helix Mimetics Based on a 1,2-Diphenylacetylene Scaffold

In order to mimic amphipathic α-helices, a novel scaffold based on a 1,2-diphenylacetylene was designed. NMR and computational modeling confirmed that an intramolecular hydrogen bond favors conformations of the 1,2-diphenylacetylene that allow for accurate mimicry of the <i>i</i>, <i>i</i> + 7 and <i>i</i> + 2, <i>i</i> + 5 side chains found on opposing faces of an α-helix

Perturbation of the c‑Myc–Max Protein–Protein Interaction via Synthetic α‑Helix Mimetics

The rational design of inhibitors of the bHLH-ZIP oncoprotein c-Myc is hampered by a lack of structure in its monomeric state. We describe herein the design of novel, low-molecular-weight, synthetic α-helix mimetics that recognize helical c-Myc in its transcriptionally active coiled-coil structure in association with its obligate bHLH-ZIP partner Max. These compounds perturb the heterodimer’s binding to its canonical E-box DNA sequence without causing protein–protein dissociation, heralding a new mechanistic class of “direct” c-Myc inhibitors. In addition to electrophoretic mobility shift assays, this model was corroborated by further biophysical methods, including NMR spectroscopy and surface plasmon resonance. Several compounds demonstrated a 2-fold or greater selectivity for c-Myc–Max heterodimers over Max–Max homodimers with IC₅₀ values as low as 5.6 μM. Finally, these compounds inhibited the proliferation of c-Myc-expressing cell lines in a concentration-dependent manner that correlated with the loss of expression of a c-Myc-dependent reporter plasmid despite the fact that c-Myc–Max heterodimers remained intact