scholarly journals Photo‐induced and Rapid Labeling of Tetrazine‐Bearing Proteins via Cyclopropenone‐Caged Bicyclononynes

2019 ◽  
Vol 58 (44) ◽  
pp. 15876-15882 ◽  
Author(s):  
Susanne V. Mayer ◽  
Anton Murnauer ◽  
Marie‐Kristin Wrisberg ◽  
Marie‐Lena Jokisch ◽  
Kathrin Lang
Keyword(s):  
2016 ◽  
Vol 6 (1) ◽  
Author(s):  
S. Shashank Chetty ◽  
S. Praneetha ◽  
Sandeep Basu ◽  
Chetana Sachidanandan ◽  
A. Vadivel Murugan

Abstract Near-infrared (NIR) luminescent CuInS2-ZnS alloyed nanocrystals (CIZS-NCs) for highly fluorescence bioimaging have received considerable interest in recent years. Owing, they became a desirable alternative to heavy-metal based-NCs and organic dyes with unique optical properties and low-toxicity for bioimaging and optoelectronic applications. In the present study, bright and robust CIZS-NCs have been synthesized within 5 min, as-high-as 230 °C without requiring any inert-gas atmosphere via microwave-solvothermal (MW-ST) method. Subsequently, the in vitro and in vivo nano-xenotoxicity and cellular uptake of the MUA-functionalized CIZS-NCs were investigated in L929, Vero, MCF7 cell lines and zebrafish-embryos. We observed minimal toxicity and acute teratogenic consequences upto 62.5 μg/ml of the CIZS-NCs in zebrafish-embryos. We also observed spontaneous uptake of the MUA-functionalized CIZS-NCs by 3 dpf older zebrafish-embryos that are evident through bright red fluorescence-emission at a low concentration of 7.8 μg/mL. Hence, we propose that the rapid, low-cost, large-scale “sustainable” MW-ST synthesis of CIZS-NCs, is an ideal bio-nanoprobe with good temporal and spatial resolution for rapid labeling, long-term in vivo tracking and intravital-fluorescence-bioimaging (IVBI).


2020 ◽  
Vol 25 (4) ◽  
pp. 356-366
Author(s):  
Wei-Ting Hung ◽  
Yi-Ting Chen ◽  
Chung-Hsuan Chen ◽  
Yuan Chuan Lee ◽  
Jim-Min Fang ◽  
...  

This study demonstrates the utilization of a flow chemistry system for continuous glycan hydrolysis and saccharide labeling to assist with the existing methods in glycan structural analysis. Acidic hydrolysis of glycans could be accelerated in a flow system. Aldoses and α-ketoacid-type saccharides were effectively labeled with naphthalene-2,3-diamine (NADA) at 60 °C for 10 min to form the fluorescent naphthimidazole (NAIM) and quinoxalinone (QXO) derivatives, respectively. The NADA-labeled derivatives improved the structural determination and composition analysis for their parent saccharides by using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS), liquid chromatography mass spectrometry (LC-MS), and nuclear magnetic resonance (NMR). Furthermore, this protocol was applied to determine the SA–Gal–Glc sequence of GM3-sugar out of six possible permutations.


2015 ◽  
Vol 113 (3) ◽  
pp. 497-502 ◽  
Author(s):  
Marie-Aude Plamont ◽  
Emmanuelle Billon-Denis ◽  
Sylvie Maurin ◽  
Carole Gauron ◽  
Frederico M. Pimenta ◽  
...  

This paper presents Yellow Fluorescence-Activating and absorption-Shifting Tag (Y-FAST), a small monomeric protein tag, half as large as the green fluorescent protein, enabling fluorescent labeling of proteins in a reversible and specific manner through the reversible binding and activation of a cell-permeant and nontoxic fluorogenic ligand (a so-called fluorogen). A unique fluorogen activation mechanism based on two spectroscopic changes, increase of fluorescence quantum yield and absorption red shift, provides high labeling selectivity. Y-FAST was engineered from the 14-kDa photoactive yellow protein by directed evolution using yeast display and fluorescence-activated cell sorting. Y-FAST is as bright as common fluorescent proteins, exhibits good photostability, and allows the efficient labeling of proteins in various organelles and hosts. Upon fluorogen binding, fluorescence appears instantaneously, allowing monitoring of rapid processes in near real time. Y-FAST distinguishes itself from other tagging systems because the fluorogen binding is highly dynamic and fully reversible, which enables rapid labeling and unlabeling of proteins by addition and withdrawal of the fluorogen, opening new exciting prospects for the development of multiplexing imaging protocols based on sequential labeling.


1980 ◽  
Vol 239 (3) ◽  
pp. G133-G135 ◽  
Author(s):  
J. H. Meyer

The lack of reliably quantitative methods has delayed understanding how the stomach empties and processes foods. Rapid refinement of gamma cameras has prompted the development of several methods for labeling of ordinary foods with radionuclides. These methods allow rapid labeling with tightly adherent nuclides and are safe for studies both in animals and humans. Nuclide-labeled foods have also permitted detailed analyses of gastric emptying in animals prepared with chronic duodenal fistulas. Early results indicate that the stomach retains foods until these are fragmented into particles smaller than 0.5 mm in diameter, and that this sieving is achieved in the antral region of the stomach. The speed of fragmentation of foods into particles of this size as well as the speed of emptying appear to be closely regulated by chemoceptive mechanisms in the small intestine, which can inhibit these processes. Thus, chemical composition of the meal regulates gastric emptying as well as the physical nature of the food, which determines how easily it can be fragmented by the stomach.


1975 ◽  
Vol 66 (3) ◽  
pp. 577-585 ◽  
Author(s):  
A Royal ◽  
R Simard

A correlated autoradiographic and biochemical study of RNA synthesis in the nucleoli of chinese hamster ovary cells has been made. Quantitative analysis of the labeling indicates that the fibrillar ribonucleoprotein (RNP) component is labeled faster than 80S RNP and 45S RNA molecules, but approaches simultaneously a steady-state 3H to 14C ratio or grains/mum2 after 30 min of [3H]uridine incorporation. On the other hand, the 55S RNP, the 36S + 32S RNA, and the granular RNP components have the same kinetic of labeling with [3H]uridine. These results suggest that the fibrillar and granular RNP components of the nucleolus are the ultrastructural substratum of, respectively, the 80S RNP (45S RNA) and 55S RNP (36S + 32S RNA). The possibility that precursors to 80S RNP exist also in the fibrillar region of the nucleolus is strongly suggested by the rapid labeling of the fibrils on the autoradiographs.


2021 ◽  
Author(s):  
Saman Enayati ◽  
Ziyu Yang ◽  
Benjamin Lu ◽  
Slobodan Vucetic

Author(s):  
Xingang Liu ◽  
Min Wu ◽  
Meng Wang ◽  
Yukun Duan ◽  
Chi Uyen Phan ◽  
...  

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