scholarly journals Ligand-directed dibromophenyl benzoate chemistry for rapid and selective acylation of intracellular natural proteins

2015 ◽  
Vol 6 (5) ◽  
pp. 3217-3224 ◽  
Author(s):  
Yousuke Takaoka ◽  
Yuki Nishikawa ◽  
Yuki Hashimoto ◽  
Kenta Sasaki ◽  
Itaru Hamachi
Keyword(s):  
Living Cells ◽  
Protein Labeling ◽  
Natural Protein ◽  
Protein Imaging ◽  
Selective Acylation ◽  
Labeling Method

A rapid and selective protein labeling method, LDBB chemistry is a useful tool for natural protein imaging in living cells.

scholarly journals Physiological Study of Lactobacillus delbrueckii subsp. bulgaricus Strains in a Novel Chemically Defined Medium

2000 ◽  
Vol 66 (12) ◽  
pp. 5306-5311 ◽  
Author(s):  
Christian Chervaux ◽  
S. Dusko Ehrlich ◽  
Emmanuelle Maguin
Keyword(s):  
Carbon Sources ◽  
Streptococcus Thermophilus ◽  
Defined Medium ◽  
Lactobacillus Delbrueckii ◽  
Protein Labeling ◽  
Chemically Defined Medium ◽  
Phosphotransferase System ◽  
Nutritional Conditions ◽  
Labeling Method

ABSTRACT We developed a chemically defined medium called milieu proche du lait (MPL), in which 22 Lactobacillus delbrueckii subsp.bulgaricus (L. bulgaricus) strains exhibited growth rates ranging from 0.55 to 1 h−1. MPL can also be used for cultivation of other lactobacilli and Streptococcus thermophilus. The growth characteristics of L. bulgaricus in MPL containing different carbon sources were determined, including an initial characterization of the phosphotransferase system transporters involved. For the 22 tested strains, growth on lactose was faster than on glucose, mannose, and fructose. Lactose concentrations below 0.4% were limiting for growth. We isolated 2-deoxyglucose-resistant mutants from strains CNRZ397 and ATCC 11842. CNRZ397-derived mutants were all deficient for glucose, fructose, and mannose utilization, indicating that these three sugars are probably transported via a unique mannose-specific-enzyme-II-like transporter. In contrast, mutants of ATCC 11842 exhibited diverse phenotypes, suggesting that multiple transporters may exist in that strain. We also developed a protein labeling method and verified that exopolysaccharide production and phage infection can occur in MPL. The MPL medium should thus be useful in conducting physiological studies ofL. bulgaricus and other lactic acid bacteria under well controlled nutritional conditions.

scholarly journals Microarrays as Model Biosensor Platforms to Investigate the Structure and Affinity of Aptamers

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Jennifer A. Martin ◽  
Yaroslav Chushak ◽  
Jorge L. Chávez ◽  
Joshua A. Hagen ◽  
Nancy Kelley-Loughnane
Keyword(s):  
Minimum Distance ◽  
Limit Of Detection ◽  
Signal To Noise Ratio ◽  
Protein Labeling ◽  
Target Interaction ◽  
Starting Conditions ◽  
Recognition Elements ◽  
Labeling Method ◽  
Biosensor Applications ◽  
Magnitude Improvement

Immobilization of nucleic acid aptamer recognition elements selected free in solution onto the surface of biosensor platforms has proven challenging. This study investigated the binding of multiple aptamer/target pairs immobilized on a commercially available microarray as a model system mimicking biosensor applications. The results indicate a minimum distance (linker length) from the surface and thymine nucleobase linker provides reproducible binding across varying conditions. An indirect labeling method, where the target was labeled with a biotin followed by a brief Cy3-streptavidin incubation, provided a higher signal-to-noise ratio and over two orders of magnitude improvement in limit of detection, compared to direct Cy3-protein labeling. We also showed that the affinities of the aptamer/target interaction can change between direct and indirect labeling and conditions to optimize for the highest fluorescence intensity will increase the sensitivity of the assay but will not change the overall affinity. Additionally, some sequences which did not initially bind demonstrated binding when conditions were optimized. These results, in combination with studies demonstrating enhanced binding in nonselection buffers, provided insights into the structure and affinity of aptamers critical for biosensor applications and allowed for generalizations in starting conditions for researchers wishing to investigate aptamers on a microarray surface.

Multicolor Protein Labeling in Living Cells Using Mutant β-Lactamase-Tag Technology

2010 ◽  
Vol 21 (12) ◽  
pp. 2320-2326 ◽  
Author(s):  
Shuji Watanabe ◽  
Shin Mizukami ◽  
Yuichiro Hori ◽  
Kazuya Kikuchi
Keyword(s):  
Living Cells ◽  
Protein Labeling

scholarly journals Organelle-Targetable Fluorescent Probes for Imaging Hydrogen Peroxide in Living Cells via SNAP-Tag Protein Labeling

2010 ◽  
Vol 132 (12) ◽  
pp. 4455-4465 ◽  
Author(s):  
Duangkhae Srikun ◽  
Aaron E. Albers ◽  
Christine I. Nam ◽  
Anthony T. Iavarone ◽  
Christopher J. Chang
Keyword(s):  
Hydrogen Peroxide ◽  
Fluorescent Probes ◽  
Living Cells ◽  
Protein Labeling

Novel post-digest isotope coded protein labeling method for phospho- and glycoproteome analysis

2010 ◽  
Vol 73 (10) ◽  
pp. 1986-2005 ◽  
Author(s):  
M. Fleron ◽  
Y. Greffe ◽  
D. Musmeci ◽  
A.C. Massart ◽  
V. Hennequiere ◽  
...  
Keyword(s):  
Protein Labeling ◽  
Labeling Method

scholarly journals A Universal Chemical Method for Rational Design of Protein-based Nanoreactors

2021 ◽  
Author(s):  
Mullapudi Mohan Reddy ◽  
Punita Bathla ◽  
Britto S. Sandanaraj
Keyword(s):  
Self Assembly ◽  
Rational Design ◽  
Chemical Method ◽  
Living Cells ◽  
Protein Labeling ◽  
Self Assembling ◽  
Naturally Occurring ◽  
General Chemical ◽  
Chemical Strategy ◽  
Artificial Protein

AbstractSelf-assembly of a monomeric protease to form a multi-subunit protein complex “proteasome” enables targeted protein degradation in living cells. The naturally occurring proteasomes serve as an inspiration and blueprint for the design of artificial protein-based nanoreactors. Here we disclose a general chemical strategy for the design of proteasome-like nanoreactors. Micelle-assisted protein labeling (MAPLab) technology along with the N-terminal bioconjugation strategy is utilized for the synthesis of a well-defined monodisperse self-assembling semi-synthetic protease. The designer protein is programmed to self-assemble into a proteasome-like nanostructure which preserves the functional properties of native protease.

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