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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Modified-Release Drug Delivery Systems: Stimuli-Activated

Stimuli-activated drug delivery systems are designed to release drugs in response to specific physical, chemical, or biological stimuli. These systems often utilize hydrogels—three-dimensional, hydrophilic polymer networks capable of swelling in aqueous environments and retaining significant fluid volumes. Upon exposure to particular stimuli, these hydrogels undergo structural transitions that allow the embedded drug to be released. Due to this adaptive behavior, such systems are also called...
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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Smart vaults: thermally-responsive protein nanocapsules.

Nicholas M Matsumoto1, Panchami Prabhakaran, Leonard H Rome

  • 1Department of Chemistry and Biochemistry and California Nanosystems Institute, 607 Charles E. Young Drive East, University of California, Los Angeles, California 90095-1569, USA.

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Researchers created novel biohybrid materials by attaching smart polymers to protein cages (vaults). These vault nanocapsules show reversible aggregation when heated, maintaining structural integrity for potential biomedical applications.

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Preparation of Multifunctional Silk-Based Microcapsules Loaded with DNA Plasmids Encoding RNA Aptamers and Riboswitches
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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Protein Engineering

Background:

  • Vaults are ubiquitous ribonucleoprotein particles forming a protein cage.
  • Recombinant vaults are structurally identical to native vaults but lack internal content.
  • Stimuli-responsive polymers offer tunable material properties.

Purpose of the Study:

  • To synthesize novel biohybrid materials using recombinant vaults and stimuli-responsive polymers.
  • To investigate the structural and responsive properties of the resulting vault nanocapsules.
  • To explore potential applications in biomedical and biotechnology fields.

Main Methods:

  • Conjugation of poly(N-isopropylacrylamide) (pNIPAAm) to engineered recombinant vaults (CP-MVP).
  • Synthesis of pNIPAAm using reversible addition-fragmentation chain transfer (RAFT) polymerization with specific end-group modifications.
  • Characterization of vault nanocapsules using electron microscopy, dynamic light scattering, and UV-vis turbidity analysis.

Main Results:

  • Successful synthesis of vault nanocapsules with conjugated pNIPAAm.
  • Demonstrated reversible aggregation of nanocapsules upon heating above the polymer's lower critical solution temperature (LCST).
  • Preservation of the vault protein cage structure throughout the thermal phase transition.

Conclusions:

  • The developed biohybrid vault nanocapsules exhibit stimuli-responsive behavior while maintaining structural integrity.
  • This new class of materials holds promise for diverse biomedical and biotechnology applications.
  • Synthetic modification of protein cages offers a versatile platform for advanced material design.