1151666-45-3Relevant articles and documents
Second Generation G-Quadruplex Stabilizing Trimethine Cyanines
Owens, Eric A.,Huynh, Hang T.,Stroeva, Ekaterina M.,Barman, Arghya,Ziabrev, Kostiantyn,Paul, Ananya,Nguyen, Sarah V.,Laramie, Matthew,Hamelberg, Donald,Germann, Markus W.,Wilson, W. David,Henary, Maged
, p. 2647 - 2663 (2019)
G-Quadruplex DNA has been recognized as a highly appealing target for the development of new selective chemotherapeutics, which could result in markedly reduced toxicity toward normal cells. In particular, the cyanine dyes that bind selectively to G-quadruplex structures without targeting duplex DNA have attracted attention due to their high amenability to structural modifications that allows fine-tuning of their biomolecular interactions. We have previously reported pentamethine and symmetric trimethine cyanines designed to effectively bind G-quadruplexes through end stacking interactions. Herein, we are reporting a second generation of drug candidates, the asymmetric trimethine cyanines. These have been synthesized and evaluated for their quadruplex binding properties. Incorporating a benz[c,d]indolenine heterocyclic unit increased overall quadruplex binding, and elongating the alkyl length increases the quadruplex-to-duplex binding specificity.
Synthesis and evaluation of carbocyanine dyes as PRMT inhibitors and imaging agents
Sinha, Sarmistha Halder,Owens, Eric A.,Feng, You,Yang, Yutao,Xie, Yan,Tu, Yaping,Henary, Maged,Zheng, Yujun George
experimental part, p. 647 - 659 (2012/09/08)
Protein arginine methylation regulates multiple biological processes. Deregulation of protein arginine methyltransferase (PRMT) activities has been observed in many disease phenotypes. Small molecule probes that target PRMTs with strong affinity and selectivity can be used as valuable tools to dissect biological mechanisms of arginine methylation and establish the role of PRMT proteins in a disease process. In this work, we report synthesis and evaluation of a class of carbocyanine compounds containing indolium, benz[e]indolium or benz[c,d]indolium heterocyclic moieties that bind to the predominant arginine methyltransferase PRMT1 and inhibit its methyltransferase activity at low micromolar potencies. In particular, the developed molecules have long wavelength colorimetric and fluorometric photoactivities, which can be used for optical and near-infrared fluorescence imaging in cells or biological tissues. Together, these new chemical probes have potential application in PRMT studies both as enzyme inhibitors and as fluorescent dyes for microscope imaging.
