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Solving the supply ...
Solving the supply of resveratrol tetramers from Papua New Guinean rainforest anisoptera species that inhibit bacterial type Ill secretion systems
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Davis, Rohan A. (author)
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Beattie, Karren D. (author)
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Xu, Min (author)
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Yang, Xinzhou (author)
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Yin, Sheng (author)
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Holla, Harish (author)
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Healy, Peter C. (author)
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Sykes, Melissa (author)
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Shelper, Todd (author)
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Avery, Vicky M. (author)
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- Elofsson, Mikael (author)
- Umeå universitet,Kemiska institutionen
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- Sundin, Charlotta (author)
- Umeå universitet,Kemiska institutionen,Creative Antibiotics Sweden AB, Umeå, Sweden
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Quinn, Ronald J. (author)
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(creator_code:org_t)
- 2014-11-18
- 2014
- English.
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In: Journal of natural products (Print). - Washington : American Chemical Society (ACS). - 0163-3864 .- 1520-6025. ; 77:12, s. 2633-2640
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http://eprints.usq.e...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
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- ABSTRACT: The supply of (−)-hopeaphenol (1) was achieved via enzymatic biotransformation in order to provide material for preclinical investigation. High-throughput screen- ing of a prefractionated natural product library aimed to identify compounds that inhibit the bacterial virulence type III secretion system (T3SS) identified several fractions derived from two Papua New Guinean Anisoptera species, showing activity against Yersinia pseudotuberculosis outer proteins E and H (YopE and YopH). Bioassay-directed isolation from the leaves of A. thurifera, and similarly A. polyandra, resulted in three known resveratrol tetramers, (−)-hopeaphenol (1), vatalbinoside A (2), and vaticanol B (3). Compounds 1−3 displayed IC50 values of 8.8, 12.5, and 9.9 μM in a luminescent reporter-gene assay (YopE) and IC50 values of 2.9, 4.5, and 3.3 μM in an enzyme-based YopH assay, respectively, which suggested that they could potentially act against the T3SS in Yersinia. The structures of 1−3 were confirmed through a combination of spectrometric, chemical methods, and single-crystal X-ray structure determinations of the natural product 1 and the permethyl ether analogue of 3. The enzymatic hydrolysis of the β-glycoside 2 to the aglycone 1 was achieved through biotransformation using the endogenous leaf enzymes. This significantly enhanced the yield of the target bioactive natural product from 0.08% to 1.3% and facilitates ADMET studies of (−)-hopeaphenol (1).
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- III secretion
- pseudomonas aeruginosa
- stem bark
- chlamydia trachomatis
- targeting virulence
- stilbene oligomers
- protein secretion
- in vivo
- yersinia
- hopeaphenol
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Davis, Rohan A.
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Beattie, Karren ...
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Xu, Min
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Yang, Xinzhou
-
Yin, Sheng
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Holla, Harish
-
show more...
-
Healy, Peter C.
-
Sykes, Melissa
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Shelper, Todd
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Avery, Vicky M.
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Elofsson, Mikael
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Sundin, Charlott ...
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Quinn, Ronald J.
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
- Articles in the publication
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Journal of natur ...
- By the university
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Umeå University