Indication of a Very Large Proton Diffusion in Ice Ih. 2. Fluorescence Quenching of Flavin Mononucleotide by Protons

2008 ◽  
Vol 112 (46) ◽  
pp. 18189-18200 ◽  
Author(s):  
Anna Uritski ◽  
Itay Presiado ◽  
Dan Huppert
Keyword(s):  
Fluorescence Quenching ◽  
Flavin Mononucleotide ◽  
Proton Diffusion

Detection of flavin mononucleotide using silver nanorod array with simultaneous Raman scattering enhancement and fluorescence quenching

2019 ◽  
Vol 58 (08) ◽  
pp. 1 ◽  
Author(s):  
Kangzhen Tian ◽  
Wen Wang ◽  
Xun Wang ◽  
Si Chen ◽  
Junqing Zhao ◽  
...  
Keyword(s):  
Fluorescence Quenching ◽  
Raman Scattering ◽  
Nanorod Array ◽  
Flavin Mononucleotide

Measurement of Large Proton Diffusion in Methanol-Doped Ice by Fluorescence Quenching of Riboflavin

2009 ◽  
Vol 113 (18) ◽  
pp. 7870-7881 ◽  
Author(s):  
Anna Uritski ◽  
Itay Presiado ◽  
Dan Huppert
Keyword(s):  
Fluorescence Quenching ◽  
Proton Diffusion

Fluorescence Quenching Reaction of Fenaminosulf with Acriflavine and Their Analytical Applications

2012 ◽  
Vol 29 (4) ◽  
pp. 440
Author(s):  
Yaqiong WANG ◽  
Shaopu LIU ◽  
Zhongfang LIU ◽  
Xiaoli HU
Keyword(s):  
Fluorescence Quenching ◽  
Analytical Applications

Characterization of Graphene Oxide Suspension for Fluorescence Quenching in DNA-Diagnostics

2016 ◽  
Vol 26 (1) ◽  
pp. 1-7 ◽  
Author(s):  
A.N. Kapitonov ◽  
G.N. Alexandrov ◽  
F.D. Vasileva ◽  
S.A. Smagulova ◽  
V.B. Timofeev ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Fluorescence Quenching ◽  
Dna Diagnostics

The Inhibition of Polysialyltranseferase ST8SiaIV Through Heparin Binding to Polysialyltransferase Domain (PSTD)

2019 ◽  
Vol 15 (5) ◽  
pp. 486-495 ◽  
Author(s):  
Li-Xin Peng ◽  
Xue-Hui Liu ◽  
Bo Lu ◽  
Si-Ming Liao ◽  
Feng Zhou ◽  
...  
Keyword(s):  
Fluorescence Quenching ◽  
Polysialic Acid ◽  
Neuronal Cell ◽  
Cd Spectroscopy ◽  
Migration And Invasion ◽  
Heparin Binding ◽  
Clinical Prognosis ◽  
Quenching Analysis ◽  
Different Types ◽  
Α Helix

Background:The polysialic acid (polySia) is a unique carbohydrate polymer produced on the surface Of Neuronal Cell Adhesion Molecule (NCAM) in a number of cancer cells, and strongly correlates with the migration and invasion of tumor cells and with aggressive, metastatic disease and poor clinical prognosis in the clinic. Its synthesis is catalyzed by two polysialyltransferases (polySTs), ST8SiaIV (PST) and ST8SiaII (STX). Selective inhibition of polySTs, therefore, presents a therapeutic opportunity to inhibit tumor invasion and metastasis due to NCAM polysialylation. Heparin has been found to be effective in inhibiting the ST8Sia IV activity, but no clear molecular rationale. It has been found that polysialyltransferase domain (PSTD) in polyST plays a significant role in influencing polyST activity, and thus it is critical for NCAM polysialylation based on the previous studies.Objective:To determine whether the three different types of heparin (unfractionated hepain (UFH), low molecular heparin (LMWH) and heparin tetrasaccharide (DP4)) is bound to the PSTD; and if so, what are the critical residues of the PSTD for these binding complexes?Methods:Fluorescence quenching analysis, the Circular Dichroism (CD) spectroscopy, and NMR spectroscopy were used to determine and analyze interactions of PSTD-UFH, PSTD-LMWH, and PSTD-DP4.Results:The fluorescence quenching analysis indicates that the PSTD-UFH binding is the strongest and the PSTD-DP4 binding is the weakest among these three types of the binding; the CD spectra showed that mainly the PSTD-heparin interactions caused a reduction in signal intensity but not marked decrease in α-helix content; the NMR data of the PSTD-DP4 and the PSTDLMWH interactions showed that the different types of heparin shared 12 common binding sites at N247, V251, R252, T253, S257, R265, Y267, W268, L269, V273, I275, and K276, which were mainly distributed in the long α-helix of the PSTD and the short 3-residue loop of the C-terminal PSTD. In addition, three residues K246, K250 and A254 were bound to the LMWH, but not to DP4. This suggests that the PSTD-LMWH binding is stronger than the PSTD-DP4 binding, and the LMWH is a more effective inhibitor than DP4.Conclusion:The findings in the present study demonstrate that PSTD domain is a potential target of heparin and may provide new insights into the molecular rationale of heparin-inhibiting NCAM polysialylation.

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