25030-19-7Relevant academic research and scientific papers
Synthesis of Triazole-Linked Analogues of c-di-GMP and Their Interactions with Diguanylate Cyclase
Fernicola, Silvia,Torquati, Ilaria,Paiardini, Alessandro,Giardina, Giorgio,Rampioni, Giordano,Messina, Marco,Leoni, Livia,Del Bello, Fabio,Petrelli, Riccardo,Rinaldo, Serena,Cappellacci, Loredana,Cutruzzolaì, Francesca
, p. 8269 - 8284 (2015/11/09)
Cyclic di-GMP (c-di-GMP) is a widespread second messenger that plays a key role in bacterial biofilm formation. The compound's ability to assume multiple conformations allows it to interact with a diverse set of target macromolecules. Here, we analyzed the binding mode of c-di-GMP to the allosteric inhibitory site (I-site) of diguanylate cyclases (DGCs) and compared it to the conformation adopted in the catalytic site of the EAL phosphodiesterases (PDEs). An array of novel molecules has been designed and synthesized by simplifying the native c-di-GMP structure and replacing the charged phosphodiester backbone with an isosteric nonhydrolyzable 1,2,3-triazole moiety. We developed the first neutral small molecule able to selectively target DGCs discriminating between the I-site of DGCs and the active site of PDEs; this molecule represents a novel tool for mechanistic studies, particularly on those proteins bearing both DGC and PDE modules, and for future optimization studies to target DGCs in vivo.
The use of a peptidic scaffold for the formation of stable guanine tetrads: Control of a H-bonded pattern in water
Murat, Pierre,Gennaro, Beatrice,Garcia, Julian,Spinelli, Nicolas,Dumy, Pascal,Defrancq, Eric
supporting information; experimental part, p. 5791 - 5795 (2011/06/21)
With a little help from a scaffold: The pre-organization of guanine units onto a peptidic scaffold allows a remarkable stabilization of the G-quartet motif (see graphic). Indeed, the quartet motif was found to be stable even in water without addition of s
