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Sökning: onr:"swepub:oai:DiVA.org:umu-104151" > Solving the supply ...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003864naa a2200589 4500
001oai:DiVA.org:umu-104151
003SwePub
008150608s2014 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1041512 URI
0247 a https://doi.org/10.1021/np500433z2 DOI
040 a (SwePub)umu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Davis, Rohan A.4 aut
2451 0a Solving the supply of resveratrol tetramers from Papua New Guinean rainforest anisoptera species that inhibit bacterial type Ill secretion systems
264 c 2014-11-18
264 1a Washington :b American Chemical Society (ACS),c 2014
338 a print2 rdacarrier
520 a 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).
650 7a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe
650 7a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng
650 7a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng
653 a III secretion
653 a pseudomonas aeruginosa
653 a stem bark
653 a chlamydia trachomatis
653 a targeting virulence
653 a stilbene oligomers
653 a protein secretion
653 a in vivo
653 a yersinia
653 a hopeaphenol
7001 a Beattie, Karren D.4 aut
7001 a Xu, Min4 aut
7001 a Yang, Xinzhou4 aut
7001 a Yin, Sheng4 aut
7001 a Holla, Harish4 aut
7001 a Healy, Peter C.4 aut
7001 a Sykes, Melissa4 aut
7001 a Shelper, Todd4 aut
7001 a Avery, Vicky M.4 aut
7001 a Elofsson, Mikaelu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)miel0001
7001 a Sundin, Charlottau Umeå universitet,Kemiska institutionen,Creative Antibiotics Sweden AB, Umeå, Sweden4 aut0 (Swepub:umu)chasun99
7001 a Quinn, Ronald J.4 aut
7102 a Umeå universitetb Kemiska institutionen4 org
7730 t Journal of natural products (Print)d Washington : American Chemical Society (ACS)g 77:12, s. 2633-2640q 77:12<2633-2640x 0163-3864x 1520-6025
8564 u http://eprints.usq.edu.au/25717/3/Davis_etal_JNP_2014_SV.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-104151
8564 8u https://doi.org/10.1021/np500433z

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