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Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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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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Cell Polarization by Rho Proteins01:21

Cell Polarization by Rho Proteins

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Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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Protein-protein Interfaces02:04

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Protein Buffers in Blood Plasma and Cells01:20

Protein Buffers in Blood Plasma and Cells

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The human body utilizes protein buffer systems to maintain a stable pH. These systems capitalize on the dual role of amino acids, which can act as acids or bases by accepting or releasing hydrogen ions in response to pH changes. Protein buffer systems are particularly significant in the extracellular fluid (ECF) and intracellular fluid (ICF) of active cells, where structural and functional proteins provide substantial buffering capacity.
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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

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Cell-Penetrating Protein/Corrole Nanoparticles.

Matan Soll1, Tridib K Goswami1, Qiu-Cheng Chen1

  • 1Schulich Faculty of Chemistry, Technion - Israel Institute of Technology, Haifa, 32000, Israel.

Scientific Reports
|February 21, 2019
PubMed
Summary
This summary is machine-generated.

Metallocorroles show varying cytotoxicity, correlating with VLDL binding. Novel nanoparticles enhance delivery of lipophilic drugs, improving cancer cell uptake and targeting for potential therapeutic applications.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Metallocorroles are versatile platforms for drug development and imaging agents.
  • Bioavailability and therapeutic activity are tunable via metal ion substitution and functional group modification.
  • Previous studies show promise for gallium corroles in cancer treatment and imaging.

Purpose of the Study:

  • To investigate the relationship between metallocorrole structure, cytotoxicity, and very low density lipoprotein (VLDL) affinity.
  • To develop a novel method for preparing cell-penetrating lipophilic metallocorrole/serum-protein nanoparticles (NPs).
  • To evaluate the cellular uptake and intracellular distribution of these nanoparticles in prostate cancer cells.

Main Methods:

  • Synthesized and tested bis-sulfonated metallocorroles with varying metal ions (Ga, Fe, Al, Mn, Sb, Au).
  • Assessed cytotoxicity and measured binding affinities to VLDL.
  • Developed a nanoparticle formulation using metallocorroles and serum proteins (albumin, transferrin).
  • Characterized nanoparticle size and morphology using Cryo-Transmission Electron Microscopy (Cryo-TEM).
  • Performed optical imaging studies on DU-145 prostate cancer cells.

Main Results:

  • Cytotoxicity of bis-sulfonated corroles increased in the order Ga < Fe < Al < Mn < Sb < Au.
  • Cytotoxicity correlated positively with metallocorrole affinity for VLDL.
  • Novel metallocorrole/serum-protein nanoparticles (~100 nm) were successfully prepared.
  • Nanoparticles exhibited rapid cellular uptake, slow release, and distribution to ER and lysosomes in DU-145 cells.
  • Transferrin-coated nanoparticles showed enhanced internalization by transferrin-receptor-rich cancer cells.

Conclusions:

  • Metallocorrole cytotoxicity and VLDL binding are key factors for therapeutic potential.
  • Metallocorrole/serum-protein nanoparticles offer a promising strategy to enhance bioavailability and targeting of hydrophobic drugs.
  • The developed nanoparticle preparation method may be applicable to a broader range of bioactive hydrophobic molecules.