Cooperative Intramolecular Hydrogen Bonding and Fluorescence Quenching Studies of Green Fluorescence Protein-like Chromophores
Date Issued
2014
Date
2014
Author(s)
Chang, Deng-Hsiang
Abstract
Hydrogen bond is an important noncovalent bonding that affects the structures and properties of molecules, polymers, and supramolecules. When there exists multiple hydrogen bonds in a molecule, the cooperative effect could strengthen or weaken the hydrogen bond. Hydrogen bond also plays an important role in photochemical or photophysical properties of chromophores. Green fluorescence protein (GFP) and its analogs are widely used as biological markers, partly because of the high fluorescence quantum yields. We’ve synthesized a highly fluorescent GFP-like chromophore m-DMABDI and found that the fluorescence is readily quenched by the solvent-solute hydrogen bonding in protic solvents. We also synthesized 1OH and 2OH to show that the hydrogen bonding to the carbonyl oxygen plays a more important role than that to the imino nitrogen in deactivating the excited state. To investigate the double hydrogen-bonding effect in this chromophore, we have synthesized 3OH, which has two intramolecular hydrogen bonds, for the studies of the cooperative effect. The results show that the rate constant of nonradiative decay induced by intramolecular hydrogen bonding (kHB) for 3OH is 3.41 s-1, which is larger than 1OH (2.28 s-1), 2OH (0.65 s-1), even the sum of that for 1OH and that for 2OH (2.93 s-1).
Subjects
類綠螢光蛋白發光團
分子內氫鍵
合作效應
螢光淬滅
Type
thesis
File(s)![Thumbnail Image]()
Loading...
Name
ntu-103-R01223141-1.pdf
Size
23.32 KB
Format
Adobe PDF
Checksum
(MD5):69e320288801e69d51200d1c686d8372