2015
DOI: 10.1016/j.compbiolchem.2015.09.006
|View full text |Cite
|
Sign up to set email alerts
|

Identification of chebulinic acid as potent natural inhibitor of M. tuberculosis DNA gyrase and molecular insights into its binding mode of action

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
14
0

Year Published

2017
2017
2022
2022

Publication Types

Select...
6
2

Relationship

2
6

Authors

Journals

citations
Cited by 41 publications
(14 citation statements)
references
References 41 publications
0
14
0
Order By: Relevance
“…Green tea polyphenols (tannins) [134], chebulinic acid [135] and anthraquinones [136] are natural phenolic compounds that showed inhibitory activity against DNA gyrase. EGCG from green tea can inhibit the B subunit of DNA gyrase at its ATP binding site [134].…”
Section: Introductionmentioning
confidence: 99%
“…Green tea polyphenols (tannins) [134], chebulinic acid [135] and anthraquinones [136] are natural phenolic compounds that showed inhibitory activity against DNA gyrase. EGCG from green tea can inhibit the B subunit of DNA gyrase at its ATP binding site [134].…”
Section: Introductionmentioning
confidence: 99%
“…The presence of the constrained HHDP group in chebulagic acid is considered to result in larger spatial hindrance and less molecular flexibility [24, 26]. Chebulinic acid, in contrast, which has a more favourable structure for entering the binding cavities or catalytic pockets of target proteases or enzymes, usually shows more broad-spectrum and potent biological activities (with the exception of chelation activity) [27, 28].
Fig.
…”
Section: Discussionmentioning
confidence: 99%
“…AND PHOSPHATE GROUP FROM DNA The double-stranded DNA (dsDNA) segment, the G-segment is cleavage, and religation by catalytic Tyr129 residue and is positively regulated by the decrease in the distance as observed in wild type DNA gyrase [Patel et al, 2015;Gubaev et al, 2016]. In the wild protein-DNA complex, OFX binds with high affinity and stabilizes the interaction between Tyr129 residue of protein and DNA phosphate with bond distance of 2.58 Åbefore MD simulation and 1.88 Åin post MD simulation (Fig.…”
Section: Analyzing the Distance Between Catalytic Residue Tyr129mentioning
confidence: 99%