scholarly journals Supramolecular polymer formation by cyclic dinucleotides and intercalators affects dinucleotide enzymatic processing

2016 ◽  
Vol 2 (1) ◽  
Author(s):  
Shizuka Nakayama ◽  
Jie Zhou ◽  
Yue Zheng ◽  
Henryk Szmacinski ◽  
Herman O Sintim
2020 ◽  
Vol 56 (62) ◽  
pp. 8739-8742
Author(s):  
Araya Ruengsuk ◽  
Korawit Khamphaijun ◽  
Puttipong Pananusorn ◽  
Andrew Docker ◽  
Jonggol Tantirungrotechai ◽  
...  

A facile synthesis of decatosylate pillar[5]arene is reported in excellent yield (>70%). The pendant tosylate arms function as an effective template in the synthesis and supramolecular polymer formation.


2005 ◽  
pp. 761 ◽  
Author(s):  
Michinori Takeshita ◽  
Miyuki Hayashi ◽  
Souichi Kadota ◽  
Kamrul Hossain Mohammed ◽  
Takehiko Yamato

2014 ◽  
Vol 1 (6) ◽  
pp. 703-706 ◽  
Author(s):  
Diem Ngan Tran ◽  
Dmitri Colesnic ◽  
Ségolène Adam de Beaumais ◽  
Gaëlle Pembouong ◽  
François Portier ◽  
...  

β-Cyclodextrin conjugated to adamantane forms self-inclusion complexes instead of supramolecular polymers.


2010 ◽  
Vol 10 (3) ◽  
pp. 1247-1256 ◽  
Author(s):  
Jun-Gill Kang ◽  
Jung-Sik Shin ◽  
Dong-Hee Cho ◽  
Yong-Kwang Jeong ◽  
Changmoon Park ◽  
...  

2015 ◽  
Vol 3 (47) ◽  
pp. 12186-12191 ◽  
Author(s):  
Md. Delwar Hossain ◽  
Rakesh K. Pandey ◽  
Utpal Rana ◽  
Masayoshi Higuchi

A Cd(ii)-based metallo-supramolecular polymer was first synthesizedviathe 1 : 1 complexation of Cd(ii) ions with bis(1,10-phenanthroline) bearing a fluorine moiety as a spacer. Selective sensing of Cd(ii) ions by the luminescent polymer formation was successfully achieved with sensitivity down to 8 nM concentration.


FEBS Open Bio ◽  
2018 ◽  
Vol 8 (6) ◽  
pp. 940-946
Author(s):  
Yasuhiro Isogai ◽  
Eisuke Takao ◽  
Ryuta Nakamura ◽  
Minoru Kato ◽  
Shigeki Kawabata

2019 ◽  
Vol 476 (21) ◽  
pp. 3333-3353 ◽  
Author(s):  
Malti Yadav ◽  
Kamalendu Pal ◽  
Udayaditya Sen

Cyclic dinucleotides (CDNs) have emerged as the central molecules that aid bacteria to adapt and thrive in changing environmental conditions. Therefore, tight regulation of intracellular CDN concentration by counteracting the action of dinucleotide cyclases and phosphodiesterases (PDEs) is critical. Here, we demonstrate that a putative stand-alone EAL domain PDE from Vibrio cholerae (VcEAL) is capable to degrade both the second messenger c-di-GMP and hybrid 3′3′-cyclic GMP–AMP (cGAMP). To unveil their degradation mechanism, we have determined high-resolution crystal structures of VcEAL with Ca2+, c-di-GMP-Ca2+, 5′-pGpG-Ca2+ and cGAMP-Ca2+, the latter provides the first structural basis of cGAMP hydrolysis. Structural studies reveal a typical triosephosphate isomerase barrel-fold with substrate c-di-GMP/cGAMP bound in an extended conformation. Highly conserved residues specifically bind the guanine base of c-di-GMP/cGAMP in the G2 site while the semi-conserved nature of residues at the G1 site could act as a specificity determinant. Two metal ions, co-ordinated with six stubbornly conserved residues and two non-bridging scissile phosphate oxygens of c-di-GMP/cGAMP, activate a water molecule for an in-line attack on the phosphodiester bond, supporting two-metal ion-based catalytic mechanism. PDE activity and biofilm assays of several prudently designed mutants collectively demonstrate that VcEAL active site is charge and size optimized. Intriguingly, in VcEAL-5′-pGpG-Ca2+ structure, β5–α5 loop adopts a novel conformation that along with conserved E131 creates a new metal-binding site. This novel conformation along with several subtle changes in the active site designate VcEAL-5′-pGpG-Ca2+ structure quite different from other 5′-pGpG bound structures reported earlier.


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