Synthetic studies of bi-fluorescence-labeled maltooligosaccharides as substrates for α-amylase on the basis of fluorescence resonance energy transfer (FRET)

Synthetic studies of bi-fluorescence-labeled maltooligosaccharides as substrates for α-amylase on the basis of fluorescence resonance energy transfer (FRET)
复制标题

DOI:
10.1016/j.bmc.2011.10.065
复制
发表时间:
2012-01-01
影响因子:
3.5
通讯作者:
Matsuoka, Koji
Matsuoka, Koji
中科院分区:
医学3区
文献类型:
--
作者:
Oka, Hiroyuki;Koyama, Tetsuo;Matsuoka, Koji

文献摘要

被引文献

相似文献

Please try later.
A series of bi-fluorescence-labeled maltooligosaccharides that lead to fluorescence resonance energy transfer (FRET) was systematically synthesized. Effective FRETs were observed with all of the synthesized probes. Digestion of probes having tetra-, quintet-, hexa- or hepta-saccharidic chain lengths with human saliva alpha-amylase resulted in disappearance of FRET when an excitation wavelength of at 290 nm was used followed by detection at ca. 520 nm due to emission from the dansyl moiety. However, continuous FRET was observed when probes having di- or trisaccharidic chain lengths were used as substrates. In addition to the substrate characteristics based on saccharidic chain length, the reaction rates of digestion for the substrates by amylase were different and also depended on their saccharidic chain length. (C) 2011 Elsevier Ltd. All rights reserved.