Journal
PROCESS BIOCHEMISTRY
Volume 52, Issue -, Pages 209-213Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2016.09.028
Keywords
Polydatin; Enzymatic acylation; Acyl recognition; Cell apoptosis; 2-Methyltetrahydrofuran
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Funding
- National Natural Science Foundation of China [21676114, 31501421]
- Qing Lan Project of Jiangsu Province
- Natural Science Research Project of Higher Education of Jiangsu Province [16KJB530001]
- Key Research Program of Industry and Information Technology of Huai'an [HAG2015031]
- Natural Science Foundation of Jiangsu Province [BK2012243]
- Foundation of Huaiyin Institute of Technology [HGB1401]
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Efficient lipase-mediated research work was successfully exploited for synthesizing, potential 6 ''-O-acylpolydatin prodrugs in biomass-derived 2-methyltetrahydrofuran (2-MeTHF). The results of the enzyme recognitions of nine acyl donors evidently demonstrated that the position and number of the C-C double bond in acyl chains profoundly influenced the behavior of the enzyme, which could be attributable to the resonance effect between the double bond and carbonyl group. Further investigations showed that introducing various acyl groups into the polydatin apparently enhanced its pH stability and 1-octanol-water partition coefficient (log P). With regard to the human cervical cancer siHa cell apoptosis by a flow cytometry assay, the lipophilic 6 ''-O-sorboyl-polydatin exhibited improved apoptosis-inducing capability than the parent drug. The presence of the more lipophilic sorboyl chain in the acylated derivative could account for this. (C) 2016 Elsevier Ltd. All rights reserved.
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