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Related Concept Videos

G-protein Coupled Receptors01:21

G-protein Coupled Receptors

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G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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G Protein-coupled Receptors01:15

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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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pH-Responsive Charge-Conversion Progelator Peptides.

Andrea S Carlini1,2, Wonmin Choi2, Naneki C McCallum2

  • 1Department of Chemistry & Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.

Advanced Functional Materials
|December 19, 2022
PubMed
Summary
This summary is machine-generated.

Researchers developed pH-responsive peptide hydrogels using a simple masking strategy. These injectable, self-assembling biomaterials show potential for drug delivery and small molecule encapsulation.

Keywords:
cathetercharge-conversionhemocompatiblehydrogelspH-responsivepeptidesself-assembly

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Nanotechnology

Background:

  • Self-assembling peptides (SAPs) are promising for biomaterial applications.
  • Stimuli-responsive hydrogels require precise control over assembly and disassembly.
  • Current methods for hydrogel formation can be complex and lack tunability.

Purpose of the Study:

  • To develop a simple and scalable strategy for creating stimuli-responsive peptide-based hydrogels.
  • To investigate the use of charge-conversion of SAPs for tunable pH responsiveness.
  • To explore the potential of these hydrogels for in vivo applications and small molecule encapsulation.

Main Methods:

  • Formulation of soluble, polyanionic peptides with acid-labile masking groups on lysine residues.
  • Induction of self-assembly via acid-triggered mask hydrolysis and subsequent β-sheet formation.
  • Assessment of hemocompatibility and cytotoxicity.
  • Demonstration of stimuli-induced self-assembly for dye sequestration.

Main Results:

  • Soluble peptides were formulated that readily flowed through needles and catheters.
  • Acidic conditions triggered rapid self-assembly into rehealable hydrogels.
  • The choice of masking groups allowed tuning of pH responsiveness and assembly kinetics.
  • Progelators exhibited hemocompatibility and noncytotoxicity; dye sequestration was demonstrated.

Conclusions:

  • A simple, scalable masking strategy enables the preparation of responsive, dynamic self-assembling biomaterials.
  • These peptide-based hydrogels are suitable for in vivo delivery and therapeutic applications.
  • The developed hydrogels can assemble in response to acidosis, offering potential for disease-relevant applications.