A contamination-insensitive probe for imaging specific biomolecules by secondary ion mass spectrometry.

@article{Kabatas2015ACP,
  title={A contamination-insensitive probe for imaging specific biomolecules by secondary ion mass spectrometry.},
  author={Selda Kabatas and Ingrid C Vreja and Sinem K. Saka and Carmen H{\"o}schen and Katharina Kr{\"o}hnert and Felipe Opazo and Silvio O. Rizzoli and Ulf Diederichsen},
  journal={Chemical communications},
  year={2015},
  volume={51 67},
  pages={
          13221-4
        }
}
Imaging techniques should differentiate between specific signals, from the biomolecules of interest, and non-specific signals, from the background. We present a probe containing (15)N and (14)N isotopes in approximately equal proportion, for secondary ion mass spectrometry imaging. This probe designed for a precise biomolecule analysis is insensitive to background signals. 

Figures from this paper

Boron‐Containing Probes for Non‐optical High‐Resolution Imaging of Biological Samples

Abstract Boron has been employed in materials science as a marker for imaging specific structures by electron energy loss spectroscopy (EELS) or secondary ion mass spectrometry (SIMS). It has a

Fluorinated nanobodies for targeted molecular imaging of biological samples using nanoscale secondary ion mass spectrometry

Specific labeling of cellular proteins with fluorinated nanobodies enables their visualization in nanoSIMS.

NanoSIMS chemical imaging combined with correlative microscopy for biological sample analysis.

Aptamers provide superior stainings of cellular receptors studied under super-resolution microscopy

It is concluded that aptamers could become useful fluorescent labeling tools for light microscopy and super-resolution imaging, and that their development for novel targets is imperative.

NanoSIMS for biological applications: Current practices and analyses.

The authors describe the major experimental factors that should be considered prior to NanoSIMS analysis and then provide information on best practices for data analysis and image generation, which includes an in-depth discussion of appropriate colormaps.

Optics-Free Visualization of Proteins in Single Cells by Time of Flight-Secondary Ion Mass Spectrometry Coupled with Genetically Encoded Chemical Tags

An optics-free strategy that images a specific protein in single cells by time of flight-secondary ion mass spectrometry (ToF-SIMS) following genetic incorporation of fluorine-containing unnatural amino acids as a chemical tag into the protein via genetic code expansion technique is reported.

Review of combined isotopic and optical nanoscopy

It is concluded that this type of technology, combined isotopic and optical nanoscopy, is reliable enough for mass application to cell biology.

Measuring synaptic vesicles using cellular electrochemistry and nanoscale molecular imaging

Making use of fluorescent or isotopically labelled probes enables super-resolution optical and mass spectrometric imaging of molecular composition and activity of single vesicles, which has proved advantageous in understanding the relationship between vesicle structure and function.

Non-Canonical Amino Acids as Minimal Tags for Investigating Protein Organization and Turnover

This thesis work developed a novel labeling scheme, for specific protein isotopic and fluorescence labeling (SPILL), which involves the incorporation of ncAA PRK followed by the reaction with two novel probes containing isotopes that are not normally abundant in cells, 19F and 15N.

Development of Nanobodies to Image Synaptic Proteins in Super-Resolution Microscopy

Die Entwicklung von hochauflosender Fluoreszenzmikroskopie hat in den vergangenen Jahrzehnten substanziell zur Erforschung subzellularer Strukturen beigetragen. Als ein bekanntes Beispiel kann hier

References

SHOWING 1-10 OF 17 REFERENCES

Secondary-Ion Mass Spectrometry of Genetically Encoded Targets**

This work presents a method for specific protein isotopic and fluorescence labeling (SPILL), based on a novel click reaction with isotopic probes, that can be applied to biological systems suitable for click chemistry, which include most cell-culture systems, as well as small model organisms.

Specific and quantitative labeling of biomolecules using click chemistry

The basics of chemical probing with click chemistry are explained, its recent applications in the field of quantitative biology are discussed, and the capability, significance, and future of the chemical probing of proteins is discussed, with an emphasis on the use of click chemistry in theField of the quantitative biology.

Multiplexed ion beam imaging of human breast tumors

This work has developed a method that uses secondary ion mass spectrometry to image antibodies tagged with isotopically pure elemental metal reporters to provide new insights into disease pathogenesis that will be valuable for basic research, drug discovery and clinical diagnostics.

Multi-isotope imaging mass spectrometry quantifies stem cell division and metabolism

The ‘immortal strand hypothesis’ is test, which predicts that during asymmetric stem cell division chromosomes containing older template DNA are segregated to the daughter destined to remain a stem cell, thus insuring lifetime genetic stability, and high-resolution quantification of stable isotope labels are provided.

Bioorthogonal reactions for labeling proteins.

The bioorthogonal chemistries used for labeling proteins are introduced and their utility for protein labeling is commented on before providing a perspective on future directions.

Multi-isotope imaging mass spectrometry (MIMS) reveals slow protein turnover in hair-cell stereocilia

Protein turnover is quantified by feeding animals with a 15N-labelled precursor amino acid and using multi-isotope imaging mass spectrometry to measure appearance of new protein, and surprisingly, in adult frogs and mice and in neonatal mice, in vivo and in vitro, the stereocilia were remarkably stable, incorporating newly synthesized protein at <10% per day.

Cu-catalyzed azide-alkyne cycloaddition.

The basis for the unique properties and rate enhancement for triazole formation under Cu(1) catalysis should be found in the high ∆G of the reaction in combination with the low character of polarity of the dipole of the noncatalyzed thermal reaction, which leads to a considerable activation barrier.

Adding new chemistries to the genetic code.

The development of new orthogonal aminoacyl-tRNA synthetase/tRNA pairs has led to the addition of approximately 70 unnatural amino acids to the genetic codes of Escherichia coli, yeast, and mammalian cells, which provide new opportunities to generate proteins with enhanced or novel properties and probes of protein structure and function.