Research data supporting "On the Synthesis and Reactivity of 2,3-Dihydropyrrolo[1,2-a]quinazolin- 5(1H)-ones"

NMR and IR data to support characterisation of synthetic compounds in publicationEPSRC [EP/K099494/1 and EP/K039520/1] Cambridge PhD Training Programme in Chemical Biology and Molecular Medicin

Aryl-linked imidazolidin-2-ones as non-peptidic beta-strand mimetics

We describe the design and synthesis of a non-peptidic beta-strand mimetic composed of alternating aryl and imidazolidin-2-one rings that can be adapted to display diverse side-chains. Solid- and solution-phase data together with calculations suggest that the desired conformation for side-chain mimicry is readily accessible and well-populated

Research data supporting '2,3-dihydropyrrolo[1,2-a]quinazolin-5(1H)-one inhibitors targeting bromodomains within the Switch/Sucrose Non-Fermenting complex'.

Data in support of the characterisation of compounds and their biological binding to proteins in the above manuscript. For synthesised compounds infra-red characterisation traces, HPLC traces where performed, and processed NMR files are provided. Raw files for the interaction of key compounds with PB1(5) and SMARCA2 and SMARCA4 proteins as measured by isothermal calorimetry are included. X-ray crystallography files are available through the Protein Data Bank.This work was supported by the EPSRC [grant numbers EP/K099494/1 EP/K039520/1], Wellcome Trust [grant number 092809/Z/10/Z] and the Cambridge PhD Training Programme in Molecular Medicine

Identification and Development of 2,3-Dihydropyrrolo[1,2‑<i>a</i>]quinazolin-5(1<i>H</i>)‑one Inhibitors Targeting Bromodomains within the Switch/Sucrose Nonfermenting Complex

Bromodomain containing proteins PB1, SMARCA4, and SMARCA2 are important components of SWI/SNF chromatin remodeling complexes. We identified bromodomain inhibitors that target these proteins and display unusual binding modes involving water displacement from the KAc binding site. The best compound binds the fifth bromodomain of PB1 with a <i>K</i>_D of 124 nM, SMARCA2B and SMARCA4 with <i>K</i>_D values of 262 and 417 nM, respectively, and displays excellent selectivity over bromodomains other than PB1, SMARCA2, and SMARCA4