Synthesis of butyl-isobutyl-phthalate and its interaction with alpha-glucosidase in vitro
文献类型：期刊论文
| 作者 | Liu, Ming1; Zhang, Wei2; Qiu, Lin3; Lin, Xiukun1 |
| 刊名 | JOURNAL OF BIOCHEMISTRY
 |
| 出版日期 | 2011 |
| 卷号 | 149期号:1页码:27-33 |
| 关键词 | butyl-isobutyl-phthalate alpha-glucosidase interaction docking simulation |
| ISSN号 | 0021-924X |
| 中文摘要 | Butyl-isobutyl-phthalate (BIP), isolated from the rhizoid of Laminaria japonica, is a potential alpha-glucosidase inhibitor for Type II diabetes treatment. In the present study, a synthetic route was established as a useful approach to obtain enough BIP. Fluorescence analysis, circular dichroism spectra and molecular docking methods were employed to elucidate the underlying molecular mechanisms of BIP inhibition on alpha-glucosidase. The results revealed that BIP could be synthesized in two steps and the synthesized BIP bound with alpha-glucosidase and induced conformational changes of the enzyme. The interaction between BIP and alpha-glucosidase was driven by both hydrophobic forces and hydrogen bond. The docking results indicated that the benzene ring and the isopropyl group of the BIP could fit into the hydrophobic pocket composed of Phe177, Phe157, Leu176, Leu218, Ala278 and the propyl group fitted into another nearby hydrophobic pocket formed by Trp154, Pro240, Leu174 and Ala162, respectively. This study provides useful information for the understanding of the BIP-alpha-glucosidase interaction and development of new alpha-glucosidase inhibitors. |
| 英文摘要 | Butyl-isobutyl-phthalate (BIP), isolated from the rhizoid of Laminaria japonica, is a potential alpha-glucosidase inhibitor for Type II diabetes treatment. In the present study, a synthetic route was established as a useful approach to obtain enough BIP. Fluorescence analysis, circular dichroism spectra and molecular docking methods were employed to elucidate the underlying molecular mechanisms of BIP inhibition on alpha-glucosidase. The results revealed that BIP could be synthesized in two steps and the synthesized BIP bound with alpha-glucosidase and induced conformational changes of the enzyme. The interaction between BIP and alpha-glucosidase was driven by both hydrophobic forces and hydrogen bond. The docking results indicated that the benzene ring and the isopropyl group of the BIP could fit into the hydrophobic pocket composed of Phe177, Phe157, Leu176, Leu218, Ala278 and the propyl group fitted into another nearby hydrophobic pocket formed by Trp154, Pro240, Leu174 and Ala162, respectively. This study provides useful information for the understanding of the BIP-alpha-glucosidase interaction and development of new alpha-glucosidase inhibitors. |
| 学科主题 | Biochemistry & Molecular Biology |
| 收录类别 | SCI |
| 原文出处 | 10.1093/jb/mvq110 |
| 语种 | 英语 |
| WOS记录号 | WOS:000285625600004 |
| 公开日期 | 2012-07-03 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/11956]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.So Res Inst, Birmingham, AL 35205 USA 3.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Nutr Sci, Shanghai 200031, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Ming,Zhang, Wei,Qiu, Lin,et al. Synthesis of butyl-isobutyl-phthalate and its interaction with alpha-glucosidase in vitro[J]. JOURNAL OF BIOCHEMISTRY,2011,149(1):27-33. |
| APA | Liu, Ming,Zhang, Wei,Qiu, Lin,&Lin, Xiukun.(2011).Synthesis of butyl-isobutyl-phthalate and its interaction with alpha-glucosidase in vitro.JOURNAL OF BIOCHEMISTRY,149(1),27-33. |
| MLA | Liu, Ming,et al."Synthesis of butyl-isobutyl-phthalate and its interaction with alpha-glucosidase in vitro".JOURNAL OF BIOCHEMISTRY 149.1(2011):27-33. |
入库方式： OAI收割
来源：海洋研究所
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