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Aegle marmelos

ABSTRACT: Aegle marmelos Genome sequencing and assembly

PROVIDER: PRJNA782429 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	SRR16998512_1.fastq.gz	Fastqsanger.gz
	SRR16998512_2.fastq.gz	Fastqsanger.gz

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Aegle marmelos

Project description:Aegle marmelos

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Aegle marmelos

Project description:Aegle marmelos overview

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Aegle marmelos

Project description:Aegle marmelos Raw sequence reads

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Aegle marmelos

Project description:Aegle marmelos Raw sequence reads

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Aegle marmelos

Project description:Aegle marmelos Transcriptome or Gene expression

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Project description:Aegle marmelos transcriptome

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Project description:Transcriptome Study of Aegle marmelos

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Project description:De novo transcriptome of Aegle marmelos.

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Interaction of active compounds from Aegle marmelos CORREA with histamine-1 receptor.

Project description:UnlabelledThe aim of this study is to determine the affinity of six active compounds of Aegle Marmelos Correa, they are (E, R)-Marmin, skimmianine, (S)-aegeline, aurapten, zeorin, and dustanin as antihistamines in histamine H1 receptor in comparison to cetirizin, diphenhydramine and chlorpheniramine as ligands comparison. Previously, in the in vitro study marmin obviously antagonized the histamine H1 receptor in a competitive manner.Methodsmolecular docking to determine the interaction of ligand binding to its receptor. Lower docking score indicates more stable binding to that protein.ResultsMarmin, skimmianine, aegeline, aurapten, zeorin, and dustanin were potential to develop as antihistamine agents, especially as histamine H1 receptor antagonists by interacting with amino acid residues, Asp107, Lys179, Lys191, Asn198, and Trp428 of histamine H1 receptor.ConclusionsBased on molecular docking, Amino acid residues involved in ligand protein interactions were Asp107, Lys179, Lys191, Asn198, and Trp428.

| S-EPMC3670119 | biostudies-literature

Semisynthetic studies identify mitochondria poisons from botanical dietary supplements--geranyloxycoumarins from Aegle marmelos.

Project description:Bioassay-guided isolation and subsequent structure elucidation of a Bael tree Aegle marmelos lipid extract yielded two unstable acylated geranyloxycoumarin mixtures (1-2), six geranyloxycoumarins (3-8), (+)-9'-isovaleroxylariciresinol (9), and dehydromarmeline (10). In a T47D cell-based reporter assay, 1 and 2 potently inhibited hypoxia-induced HIF-1 activation (IC50 values 0.18 and 1.10 ?gmL(-1), respectively). Insufficient material and chemical instability prevented full delineation of the fatty acyl side chain olefin substitution patterns in 1 and 2. Therefore, five fatty acyl geranyloxycoumarin ester derivatives (11-15) were prepared from marmin (3) and commercial fatty acyl chlorides by semisynthesis. The unsaturated C-6' linoleic acid ester derivative 14 that was structurally most similar to 1 and 2, inhibited HIF-1 activation with comparable potency (IC50 0.92 ?M). The octanoyl (11) and undecanoyl (12) ester derivatives also suppressed HIF-1 activation (IC50 values 3.1 and 0.87 ?M, respectively). Mechanistic studies revealed that these geranyloxycoumarin derivatives disrupt mitochondrial respiration, primarily at complex I. Thus, these compounds may inhibit HIF-1 activation by suppressing mitochondria-mediated hypoxic signaling. One surprising observation was that, while less potent, the purported cancer chemopreventive agent auraptene (8) was found to act as a mitochondrial poison that disrupts HIF-1 signaling in tumors.

| S-EPMC3602229 | biostudies-literature

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