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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
Synthesis of Phosphatidylcholine in the ER Membrane01:27

Synthesis of Phosphatidylcholine in the ER Membrane

The ER synthesizes lipids for building cell membranes and performing cellular functions such as energy storage and signaling. The lipid synthesis machinery embedded in the ER membrane primarily collects all reactants from the cytosol. Following synthesis, the secretory pathway and the ER contact sites distribute these lipids to other cellular organelles. Additionally, the energy-rich triacylglycerides are transported from the ER via lipid droplets.
The major components of all eukaryotic cell...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

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Related Experiment Video

Updated: May 20, 2026

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

pH-Dependent Interaction between C-Peptide and Phospholipid Bicelles.

Sofia Unnerståle1, Lena Mäler

  • 1Department of Biochemistry and Biophysics, Center for Biomembrane Research, The Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91 Stockholm, Sweden.

Journal of Biophysics (Hindawi Publishing Corporation : Online)
|August 1, 2012
PubMed
Summary

C-peptide remains unstructured but weakly forms beta-sheets at low pH, interacting with lipids. This pH-dependent lipid association may influence C-peptide aggregation in vivo.

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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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Published on: July 27, 2017

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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
10:26

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physical Chemistry

Background:

  • C-peptide links insulin's A and B chains within proinsulin.
  • Understanding C-peptide's biophysical interactions is crucial for its biological role.
  • Lipid interactions can significantly alter peptide structure and function.

Purpose of the Study:

  • To investigate the pH-dependent interaction between C-peptide and phospholipid bicelles.
  • To determine if C-peptide undergoes structural changes upon lipid binding.
  • To explore the implications of these interactions for C-peptide's in vivo behavior.

Main Methods:

  • Circular dichroism spectroscopy to assess peptide structure.
  • Nuclear magnetic resonance spectroscopy to study molecular interactions.
  • Utilizing neutral and acidic phospholipid bicelles to mimic cell membranes.

Main Results:

  • C-peptide is predominantly unstructured across pH ranges.
  • A minor induction of beta-sheet structure occurs at low pH (isoelectric point).
  • C-peptide associates with both neutral and acidic bicelles at low pH without significant structural rearrangement, indicating uncoupled folding and binding.

Conclusions:

  • C-peptide's interaction with lipids is pH-dependent, occurring at low pH.
  • Lipid binding does not induce major structural changes in C-peptide.
  • Environmental pH variations in vivo could lead to C-peptide-lipid association, potentially affecting peptide aggregation.