3′-Pyrene-modified unlocked nucleic acids: synthesis, fluorescence properties and a surprising stabilization effect on duplexes and triplexes

2017 ◽  
Vol 15 (9) ◽  
pp. 2073-2085 ◽  
Author(s):  
Maria Ejlersen ◽  
Niels Langkjær ◽  
Jesper Wengel

Synthesis of a novel 3′-pyrene-functionalized UNA monomer with unprecedented thermal stabilization of duplexes and triplexes.

2011 ◽  
Vol 2011 ◽  
pp. 1-13 ◽  
Author(s):  
Aishwarya Prakash ◽  
Fabien Kieken ◽  
Luis A. Marky ◽  
Gloria E. O. Borgstahl

Replication protein A (RPA) plays an essential role in DNA replication by binding and unfolding non-canonical single-stranded DNA (ssDNA) structures. Of the six RPA ssDNA binding domains (labeled A-F), RPA-CDE selectively binds a G-quadruplex forming sequence (5′-TAGGGGAAGGGTTGGAGTGGGTT-3′called Gq23). In K+, Gq23 forms a mixed parallel/antiparallel conformation, and in Na+Gq23 has a less stable (TMlowered by ∼20∘C), antiparallel conformation. Gq23 is intramolecular and 1D NMR confirms a stable G-quadruplex structure in K+. Full-length RPA and RPA-CDE-core can bind and unfold the Na+form of Gq23 very efficiently, but complete unfolding is not observed with the K+form. Studies with G-quadruplex ligands, indicate that TMPyP4 has a thermal stabilization effect on Gq23 in K+, and inhibits complete unfolding by RPA and RPA-CDE-core. Overall these data indicate that G-quadruplexes present a unique problem for RPA to unfold and ligands, such as TMPyP4, could possibly hinder DNA replication by blocking unfolding by RPA.


2002 ◽  
Vol 21 (3) ◽  
pp. 353-361 ◽  
Author(s):  
S. Jipa ◽  
T. Zaharescu ◽  
R. Setnescu ◽  
T. Setnescu ◽  
J. Herdan ◽  
...  

2004 ◽  
Vol 61 (1) ◽  
pp. 79-84 ◽  
Author(s):  
Todor Deligeorgiev ◽  
Iliana Timcheva ◽  
Vera Maximova ◽  
Nikolai Gadjev ◽  
Alexey Vassilev ◽  
...  

2015 ◽  
Vol 88 (9) ◽  
pp. 1539-1550 ◽  
Author(s):  
Jianping Liu ◽  
Xia Song ◽  
Mingpei Tang ◽  
Hongzhou Shang ◽  
Li Yan

2021 ◽  
Vol 2063 (1) ◽  
pp. 012005
Author(s):  
Hikmat A Ali ◽  
Hussein A Shnawa ◽  
Dhiaa A Abidalimam

Abstract In this study, calcium complex of anthocyanin was synthesized from anthocyanin, a flavonoid type natural phenolic product, which was extracted from eggplant peel. The structure of Ca-anthocyanin was characterized by FTIR spectroscopy. Its efficiency as bio-based thermal stabilizer to stabilize poly (vinyl chloride) was investigated and compared to that of Reapak B-NT/7060, a Ca/Zn-based commercial stabilizer. The influence of Ca-anthocyanin complex on the thermal degradation reaction of PVC was monitored by differential scanning calorimetry (DSC). The results indicated that the Ca-anthocyanin complex is an efficient thermal stabilizer and it reduces the rate of dehydrochlorination reaction of PVC already at a concentration as small as 2 phr, part per hundred of PVC resin. The thermal degradation reaction of PVC through the first degradation stage is clearly limited by the addition of Ca-anthocyanin complex as single (primary) stabilizer. Its efficiency is similar to that of Reapak B-NT/7060 used as reference stabilizer and it can enhance the performance of commercial stabilizer when used as co-stabilizer at mixing ratio (1:1). This study has allowed verifying and validating the usefulness of environmental friendly thermal stabilizer for PVC with very evident stabilization effect.


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