In silico approach of azadirachtin binding with actins

Kumar, Ram; Manoj, Madhav; Kush, Anil; Annadurai, R. S.

doi:10.1016/j.ibmb.2007.03.010

Cited by 25 publications

(16 citation statements)

References 11 publications

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“…The accompanying report on the molecular modelling of interactions between Aza and b-actin suggests that structure of b-actin in insect cell is quite distinct from that of mammalian, though the two share considerable sequence identity and similarity. Their results suggest that few differences in amino acid sequence cause stearic hinderance for Aza to bind to the mammalian b-actin pocket (Pravin kumar et al, 2007). These results further enhance the value of Aza as a potential insecticide of biological origin as well as for other biological applications.…”

Section: Discussionmentioning

confidence: 88%

Actin cytoskeleton as a putative target of the neem limonoid Azadirachtin A

Anuradha

Annadurai

Shashidhara

2007

Insect Biochemistry and Molecular Biology

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Section: Discussionmentioning

confidence: 88%

Actin cytoskeleton as a putative target of the neem limonoid Azadirachtin A

Anuradha

Annadurai

Shashidhara

2007

Insect Biochemistry and Molecular Biology

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“…Salehzadeh et al [31] found that azadirachtin had moderate to strong cytotoxicity, with antimitotic effects in Sf9 cells, which is similar to taxol and colchicine, and it is thought to target tubulin. In the Drosophila system, Anuradha et al [32] reported that azadirachtin could alter or prevent the formation of new assemblages of organelles or the cytoskeleton, especially in the eye and wing imaginal discs of D. melanogaster third instar larvae, and suggested that the actin cytoskeleton is targeted by azadirachtin in cells of the Drosophila compound eye [33]. Notably, a putative azadirachtin-binding hsp60 complex was identified in Drosophila Kc167 cells [34].…”

Section: Introductionmentioning

confidence: 99%

The Mitochondria-Mediate Apoptosis of Lepidopteran Cells Induced by Azadirachtin

Huang

et al. 2013

PLoS ONE

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Mitochondria have been shown to play an important role in apoptosis using mammalian cell lines. However, this seems not to be the case in Drosophila, an insect model organism; thus more in-depth studies of insect cell apoptosis are necessary. In the present study, mitochondrial involvement during azadirachtin- and camptothecin-induced apoptosis in Spodoptera frugiperda Sf9 cells (isolated from Spodoptera frugiperda pupal ovarian tissue) was investigated. The results showed that both azadirachtin and camptothecin could induce apoptosis in Sf9 cells. Reactive oxygen species (ROS) generation, activation of mitochondrial permeability transition pores (MPTPs) and loss of mitochondrial membrane potential (MMP) were observed very early during apoptosis and were followed subsequently by the release of cytochrome-c from the mitochondria. Furthermore, the results also revealed that the opening of MPTPs and the loss of MMP induced by azadirachtin could be significantly inhibited by the permeability transition pore (PTP) inhibitor cyclosporin A (CsA), which was used to identify the key role of mitochondria in the apoptosis of Sf9 cells. However, in camptothecin-treated Sf9 cells, CsA could not suppress the opening of MPTPs and the loss of MMP when apoptosis was induced. The data from caspase-3 and caspase-9 activity assays and detection of apoptosis by morphological observation and flow cytometry also uncovered the different effect of CsA on the two botanical apoptosis inducers. Although different mechanisms of apoptosis induction exist, our study revealed that mitochondria play a crucial role in insect cell line apoptosis.

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“…The mechanism of inhibition would mainly involve interaction of azadirachtin with one of the amino acids in the catalytic triad, which is very important for lipase activity such as aspartic acid. Using the in silico approach Pravin Kumar et al 25 showed for the first time that there is a charge‐based interaction between azadirachtin and Arg, Lys, Glu and Asp (only amino acids). The activity results clearly demonstrate that RBL inhibition is more pronounced at higher concentrations of azadirachtin.…”

Section: Resultsmentioning

confidence: 99%

Inhibition of rice bran lipase by azadirachtin from Azadirachta indica

Gaṅgādhara¹,

Kumar²,

Prakash³

2009

J Sci Food Agric

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BACKGROUND: Chemical constituents of the neem tree are extensively explored; the major component present in the tree is azadirachtin. Azadirachtin, a tetranortriterpenoid, is remarkable for its chemical complexity and for its biological activity. This study, for the first time, has provided information on the interaction and inhibition of rice bran lipase (RBL) by azadirachtin. RBL, an esterase, is a versatile enzyme that catalyzes the hydrolysis of ester linkages, primarily in neutral lipids such as triglycerides.

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In silico approach of azadirachtin binding with actins

Cited by 25 publications

References 11 publications

Actin cytoskeleton as a putative target of the neem limonoid Azadirachtin A

Actin cytoskeleton as a putative target of the neem limonoid Azadirachtin A

The Mitochondria-Mediate Apoptosis of Lepidopteran Cells Induced by Azadirachtin

Inhibition of rice bran lipase by azadirachtin from Azadirachta indica

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