scholarly journals Locked nucleic acid (LNA) enhances binding affinity of triazole-linked DNA towards RNA

2017 ◽  
Vol 53 (63) ◽  
pp. 8910-8913 ◽  
Author(s):  
Pawan Kumar ◽  
Afaf H. El-Sagheer ◽  
Lynda Truong ◽  
Tom Brown
Keyword(s):  
Nucleic Acid ◽  
Binding Affinity ◽  
Rna Binding ◽  
Locked Nucleic Acid ◽  
Enzymatic Stability

LNA improves the RNA-binding affinity and enzymatic stability of triazole-linked DNA.

C5-azobenzene-functionalized locked nucleic acid uridine: isomerization properties, hybridization ability, and enzymatic stability

2015 ◽  
Vol 13 (18) ◽  
pp. 5209-5214 ◽  
Author(s):  
K. Morihiro ◽  
O. Hasegawa ◽  
S. Mori ◽  
S. Tsunoda ◽  
S. Obika
Keyword(s):  
Nucleic Acid ◽  
Locked Nucleic Acid ◽  
Enzymatic Stability ◽  
Selective Hybridization

C5-azobenzene-functionalized locked nucleic acid uridine (LNA-UAz) shows effective photo-isomerization properties, RNA-selective hybridization ability, and high enzymatic stability.

The Eight Stereoisomers of LNA (Locked Nucleic Acid): A Remarkable Family of Strong RNA Binding Molecules

2000 ◽  
Vol 39 (9) ◽  
pp. 1656-1659 ◽  
Author(s):  
Vivek K. Rajwanshi ◽  
Anders E. Håkansson ◽  
Mads D. Sørensen ◽  
Stefan Pitsch ◽  
Sanjay K. Singh ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Rna Binding ◽  
Locked Nucleic Acid

The Eight Stereoisomers of LNA (Locked Nucleic Acid): A Remarkable Family of Strong RNA Binding Molecules

2000 ◽  
Vol 112 (9) ◽  
pp. 1722-1725 ◽  
Author(s):  
Vivek K. Rajwanshi ◽  
Anders E. Håkansson ◽  
Mads D. Sørensen ◽  
Stefan Pitsch ◽  
Sanjay K. Singh ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Rna Binding ◽  
Locked Nucleic Acid

scholarly journals Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity

2018 ◽  
Vol 92 (17) ◽  
Author(s):  
Zhe Zeng ◽  
Feng Deng ◽  
Ke Shi ◽  
Gang Ye ◽  
Gang Wang ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Crystal Structures ◽  
Binding Affinity ◽  
Disulfide Bond ◽  
Rna Binding ◽  
Critical Role ◽  
Nucleic Acid Binding ◽  
Wild Type ◽  
Dimer Interface ◽  
Diarrhea Virus

ABSTRACTCoronaviruses pose serious health threats to humans and other animals. Understanding the mechanisms of their replication has important implications for global health and economic stability. Nonstructural protein 9 (nsp9) is an essential RNA binding protein for coronavirus replication. However, the mechanisms of the dimerization and nucleic acid binding of nsp9 remain elusive. Here, we report four crystal structures, including wild-type porcine delta coronavirus (PDCoV) nsp9, PDCoV nsp9-ΔN7 (N-terminal 7 amino acids deleted), wild-type porcine epidemic diarrhea virus (PEDV) nsp9, and PEDV nsp9-C59A mutant. These structures reveal the diverse dimerization forms of coronavirus nsp9. We first found that the N-finger of nsp9 from PDCoV plays a critical role in dimerization. Meanwhile, PEDV nsp9 is distinguished by the presence of a disulfide bond in the dimer interface. Interestingly, size exclusion chromatography and analytical ultracentrifugation analyses indicate that the PDCoV nsp9-ΔN7 and PEDV nsp9-C59A mutants are monomeric in solution. In addition, electrophoretic mobility shift assays and microscale thermophoresis analysis indicate that the monomeric forms of PDCoV nsp9 and PEDV nsp9 still have nucleic acid binding affinity, although it is lower than that of the wild type. Our results show that the diverse dimerization forms of coronavirus nsp9 proteins enhance their nucleic acid binding affinity.IMPORTANCECoronaviruses cause widespread respiratory, gastrointestinal, and central nervous system diseases in humans and other animals, threatening human health and causing economic loss. Coronavirus nsp9, a member of the replication complex, is an important RNA binding subunit in the RNA-synthesizing machinery of all coronaviruses. However, the mechanisms of the dimerization and nucleic acid binding of nsp9 remain elusive. In this study we determined the nsp9 crystal structures of PDCoV and PEDV. We first found that the N-finger of nsp9 from PDCoV plays a critical role in dimerization. Meanwhile, PEDV nsp9 is distinguished by the presence of a disulfide bond in the dimer interface. This study provides a structural and functional basis for understanding the mechanism of dimerization and shows that the diverse dimerization modes of coronavirus nsp9 proteins enhance their nucleic acid binding affinity. Importantly, these findings may provide a new insight for antiviral drug development.

Trinucleotide Cap Analogue Bearing a Locked Nucleic Acid Moiety: Synthesis, mRNA Modification, and Translation for Therapeutic Applications

2021 ◽  
Author(s):  
Annamalai Senthilvelan ◽  
Tyson Vonderfecht ◽  
Muthian Shanmugasundaram ◽  
Indra Pal ◽  
Jason Potter ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Locked Nucleic Acid ◽  
Acid Moiety ◽  
Therapeutic Applications

Solution Structure of a Locked Nucleic Acid Modified Quadruplex: Introducing the V4 Folding Topology

2009 ◽  
Vol 121 (17) ◽  
pp. 3145-3149 ◽  
Author(s):  
Jakob T. Nielsen ◽  
Khalil Arar ◽  
Michael Petersen
Keyword(s):  
Nucleic Acid ◽  
Solution Structure ◽  
Locked Nucleic Acid

i-Motif Formation with Locked Nucleic Acid (LNA)

2007 ◽  
Vol 119 (48) ◽  
pp. 9380-9382 ◽  
Author(s):  
Niti Kumar ◽  
Jakob T. Nielsen ◽  
Souvik Maiti ◽  
Michael Petersen
Keyword(s):  
Nucleic Acid ◽  
Locked Nucleic Acid
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