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Related Concept Videos

Introduction to Membrane Traffic01:44

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The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
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Delivery Pathways to the Lysosome01:36

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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Overview of Protein Sorting and Transport01:45

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Cargo Loading onto Kinesin Powered Molecular Shuttles
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Intracellular targets: A multiple cargo transporting molecule.

Christos Papadopoulos1, Evgenia Fotou1, Vassilios Moussis1

  • 1Laboratory of Protein and Peptide Chemistry, Department of Chemistry, University of Ioannina, Ioannina, Greece.

Journal of Peptide Science : an Official Publication of the European Peptide Society
|June 16, 2021
PubMed
Summary

A novel peptide carrier, Cell Penetrating Sequential Oligopeptide Carrier (CPSOC), efficiently delivers functional peptides into cells. This carrier successfully inhibited Cdc42 protein activity, demonstrating its potential for targeted molecular delivery.

Keywords:
Cdc42cell-penetrating peptidesendothelial cellsfluoresceinintracellular targetingvon Willebrand factor exocytosis

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Cell-penetrating peptides (CPPs) are vital for intracellular delivery but face challenges like toxicity and endosomal entrapment.
  • Understanding CPPs' cellular entry mechanisms is crucial for optimizing drug delivery systems.

Purpose of the Study:

  • To evaluate the efficacy of a novel peptide carrier, Cell Penetrating Sequential Oligopeptide Carrier (CPSOC), in penetrating cell membranes and delivering conjugated cargo.
  • To assess the functionality of CPSOC-delivered peptides targeting the Cdc42 protein.

Main Methods:

  • CPSOC, composed of Lys-Aib-Cys moieties, was synthesized for cargo conjugation via a thioether bond.
  • The carrier's cell penetration and cargo delivery capabilities were tested.
  • Functional assays were performed using CPSOC-conjugated peptides targeting Cdc42 to inhibit exocytosis.

Main Results:

  • CPSOC demonstrated efficient cell membrane penetration and successful intracellular delivery of conjugated peptides.
  • Internalized CPSOC-conjugated Cdc42 peptides effectively inhibited exocytosis of von Willebrand factor from endothelial cells.
  • The carrier's lysine residue provided positive charge, and α-amino isobutyric acid ensured helical conformation and enzymatic stability.

Conclusions:

  • CPSOC serves as an efficient carrier for delivering functional peptides into cells.
  • This carrier system holds promise for transporting multiple cargoes and advancing intracellular delivery strategies.