title: Synthetic studies of bi-fluorescence-labeled maltooligosaccharides as substrates for α-amylase on the basis of fluorescence resonance energy transfer (FRET).
abstract: 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 α-amylase resulted in disappearance of FRET when an excitation wavelength of at 290nm was used followed by detection at ca. 520nm 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.
authors.affiliation: Division of Material Science, Graduate School of Science and Engineering, Saitama University, Sakura, Saitama 338-8570, Japan.
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Oka
authors.forename: Tetsuo
authors.initials: T
authors.lastname: Koyama
authors.forename: Ken
authors.initials: K
authors.lastname: Hatano
authors.forename: Koji
authors.initials: K
authors.lastname: Matsuoka
mesh_terms: D031541:Fluorescence Resonance Energy Transfer; D005456:Fluorescent Dyes / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D009844:Oligosaccharides / Q000138:chemical synthesis* / Q000737:chemistry; D012463:Saliva / Q000201:enzymology; D013379:Substrate Specificity; D000516:alpha-Amylases / Q000378:metabolism*
chemical_list: D005456:Fluorescent Dyes; D009844:Oligosaccharides; C021705:maltooligosaccharides; D000516:alpha-Amylases