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Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
Immunogold Electron Microscopy01:20

Immunogold Electron Microscopy

Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...

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Updated: Jul 8, 2026

Initial Evaluation of Antibody-conjugates Modified with Viral-derived Peptides for Increasing Cellular Accumulation and Improving Tumor Targeting
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Nuclear localization of HIV-1 tat functionalized gold nanoparticles.

C C Berry1, J M de la Fuente, M Mullin

  • 1Centre for Cell Engineering, Institute of Biomedical and Life Sciences, University of Glasgow, UK. Catherine.berry@bio.gla.ac.uk

IEEE Transactions on Nanobioscience
|January 26, 2008
PubMed
Summary

Researchers developed HIV-1 tat peptide-functionalized gold nanoparticles for intracellular delivery. Smaller 5 nm nanoparticles successfully entered the nucleus, while larger 30 nm ones remained in the cytoplasm, indicating size-dependent nuclear pore passage.

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Published on: October 29, 2020

Area of Science:

  • Biotechnology
  • Nanomedicine
  • Cell Biology

Background:

  • The cell plasma membrane's impermeability hinders macromolecule therapeutic delivery.
  • Protein transduction domains (PTDs), like HIV-1 tat peptide, facilitate cellular uptake and intracellular delivery.
  • Nuclear delivery of PTD-conjugated molecules and nanoparticles remains a challenge.

Purpose of the Study:

  • To develop water-soluble, biocompatible gold nanoparticles functionalized with the HIV-1 tat PTD.
  • To create novel nuclear targeting agents for enhanced intracellular delivery.
  • To investigate the effect of nanoparticle size on nuclear entry.

Main Methods:

  • Synthesized gold nanoparticles of varying sizes (5 nm and 30 nm).
  • Functionalized nanoparticles with the HIV-1 tat PTD.
  • Tested nanoparticle uptake and localization in vitro using a human fibroblast cell line.

Main Results:

  • Demonstrated successful transfer of functionalized nanoparticles across the plasma membrane.
  • Observed nuclear entry for 5 nm tat-PTD-gold nanoparticles.
  • Found that 30 nm tat-PTD-gold nanoparticles were retained in the cytoplasm.

Conclusions:

  • Nanoparticle size is a critical factor for achieving nuclear entry.
  • The observed cytoplasmic retention of larger nanoparticles suggests blockage at the nuclear pore complex.
  • These findings pave the way for developing size-optimized nanoparticles for targeted nuclear delivery.