Comparison of unfiltered and filtered <i>M. smegmatis</i>.

<p>Unfiltered <i>M. smegmatis</i> under 40x magnification (A) and plated onto agar (B); <i>M. smegmatis</i> filtered through 5-µm pore filter under 40 x magnification (C) and plated onto agar (D), scale bar applies to both A and C.</p

Recovery of <i>M. smegmatis</i> after Vortexing and Filtration.

<p>Mean ±Standard Deviation; n = 4.</p

Histogram of unfiltered, vortexed and filtered <i>M. smegmatis</i>.

<p>Distributions of resorufin fluorescence signals from 384 wells of a 384-well plate contained unfiltered (A), vortexed (B) or filtered (C) <i>M. smegmatis</i>. After the treatment, the bacteria were distributed into the 384-well plates followed by the addition of resazurin, which was converted to resorufin by the living bacteria.</p

Agreement analysis of duplicate plates from unfiltered, vortexed and filtered bacteria.

<p>Correlation of two duplicate assay plates tested against LOPAC compounds using unfiltered bacteria (A), vortexed bacteria (B) and filtered bacteria (C).</p

Structure–Activity Relationships and Kinetic Studies of Peptidic Antagonists of CBX Chromodomains

To better understand the contribution of methyl-lysine (Kme) binding proteins to various disease states, we recently developed and reported the discovery of <b>1</b> (UNC3866), a chemical probe that targets two families of Kme binding proteins, CBX and CDY chromodomains, with selectivity for CBX4 and -7. The discovery of <b>1</b> was enabled in part by the use of molecular dynamics simulations performed with CBX7 and its endogenous substrate. Herein, we describe the design, synthesis, and structure–activity relationship studies that led to the development of <b>1</b> and provide support for our model of CBX7–ligand recognition by examining the binding kinetics of our antagonists with CBX7 as determined by surface-plasmon resonance