synthesis and α-glucosidase inhibitory mechanisms of bis(2,3-dibromo-4,5-dihydroxybenzyl) ether, a potential marine bromophenol α-glucosidase inhibitor合成和α-glucosidase抑制机制的bis(2 3-dibromo-4 5-dihydroxybenzyl)醚、潜在海洋溴酚α-glucosidase抑制剂.pdfVIP

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synthesis and α-glucosidase inhibitory mechanisms of bis(2,3-dibromo-4,5-dihydroxybenzyl) ether, a potential marine bromophenol α-glucosidase inhibitor合成和α-glucosidase抑制机制的bis(2 3-dibromo-4 5-dihydroxybenzyl)醚、潜在海洋溴酚α-glucosidase抑制剂.pdf

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synthesis and α-glucosidase inhibitory mechanisms of bis(2,3-dibromo-4,5-dihydroxybenzyl) ether, a potential marine bromophenol α-glucosidase inhibitor合成和α-glucosidase抑制机制的bis(2 3-dibromo-4 5-dihydroxybenzyl)醚、潜在海洋溴酚α-glucosidase抑制剂

Mar. Drugs 2011, 9, 1554-1565; doi:10.3390/md9091554 OPEN ACCESS Marine Drugs ISSN 1660-3397 /journal/marinedrugs Article Synthesis and α-Glucosidase Inhibitory Mechanisms of Bis(2,3-dibromo-4,5-dihydroxybenzyl) Ether, a Potential Marine Bromophenol α-Glucosidase Inhibitor Ming Liu 1, Wei Zhang 2, Jianteng Wei 1 and Xiukun Lin 1,* 1 Institute of Oceanology, Chinese Academy of Science, 7 Nanhai Rd, Qingdao 266071, China; E-Mails: lmouc@ (M.L.); weijt@163.com (J.W.) 2 Southern Research Institute, 2000 9th Avenue South, Birmingham, AL 35205, USA; E-Mail: zhangwee@ * Author to whom correspondence should be addressed; E-Mail: linxiukun@; Tel./Fax: +86-532-8289-8916. Received: 1 July 2011; in revised form: 26 July 2011 / Accepted: 8 August 2011 / Published: 19 September 2011 Abstract: Bis(2,3-dibromo-4,5-dihydroxybenzyl) ether (BDDE), derived from the marine algae, is a potential α-glucosidase inhibitor for type 2 diabetes treatment. In the present study, a synthetic route was established as a valid approach to obtain BDDE. Fluorescence spectra, circular dichroism spectra and molecular docking methods were employed to elucidate the inhibitory mechanisms of BDDE against α-glucosidase. The results showed that BDDE could be prepared effectively and efficiently with the established synthetic methods. Synthetic BDDE bound with α-glucosidase and induced minor conformational changes of the enzyme. The docking results indicated the interaction between BDDE an