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Protein Dynamics in Living Cells01:19

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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19F: A small probe for a giant protein.

Lucrezia Cosottini1, Stefano Zineddu1, Lara Massai2

  • 1Magnetic Resonance Center (CERM), University of Florence, via Luigi Sacconi 6, Sesto Fiorentino 50019, Italy; Department of Chemistry "Ugo Schiff", University of Florence, via della Lastruccia 3, Sesto Fiorentino 50019, Italy.

Journal of Inorganic Biochemistry
|May 5, 2023
PubMed
Summary

We developed a method to efficiently produce fluorinated human H ferritin using 5-fluoroindole. This modified ferritin acts as a probe for studying interactions and monitoring cellular uptake in drug delivery applications.

Keywords:
(19)F NMR5-F-TrpESI-MSHuman ferritinNanocage

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Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Human H ferritin is a protein nanocage with potential applications in drug delivery.
  • Fluorine-19 (19F) labeling offers unique advantages for biomolecular studies.
  • The W93 residue in human H ferritin is surface-exposed, making it accessible for modification.

Purpose of the Study:

  • To develop an efficient method for incorporating fluorine-19 into human H ferritin.
  • To explore the utility of 5-F-Trp human H ferritin as a probe for intermolecular interactions.
  • To investigate the application of 5-F-Trp human H ferritin in monitoring cellular uptake.

Main Methods:

  • Selective incorporation of 19F into the W93 residue using 5-fluoroindole.
  • Characterization of 5-F-Trp human H ferritin using NMR spectroscopy.
  • Exploitation of intrinsic fluorescence for interaction studies.

Main Results:

  • Achieved efficient fluorination (∼90%) of human H ferritin.
  • Observed a well-defined 19F NMR resonance for the large ferritin nanocage.
  • Demonstrated the potential for chemical shift perturbation mapping of intermolecular interactions.
  • Showcased the ability to monitor ferritin uptake by cells.

Conclusions:

  • 5-F-Trp human H ferritin is efficiently produced and characterized.
  • The modified ferritin serves as a valuable tool for studying intermolecular interactions in solution.
  • This approach enables monitoring of ferritin-based drug carrier uptake in cellular systems.