Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology

Electrostatic interaction of neutral semi-permeable membranes.

We consider an osmotic equilibrium between bulk solutions of polyelectrolyte bounded by semi-permeable membranes and separated by a thin film of salt-free liquid. Although the membranes are neutral, the counter-ions of the polyelectrolyte molecules permeate into the gap and lead to a steric charge separation. This gives rise to a distance-dependent membrane potential, which translates into a re...

INTERACTION OF PROTEINS WITH SMALL MOLECULES

Interaction of cationic phosphorus dendrimers with lipid membranes

Large unilamellar liposomes and multilamellar vesicles consisting of DMPC interacted with cationic phosphorus-containing dendrimers CPDs G3 and G4. DSC and ζ -potential measurements have shown that liposomal-dendrimeric molecular recognition occurs due to the interaction between the complementary surface groups. Calorimetric studies indicate that the enthalpy of the transition of the lipids tha...

Interaction of viral oncogenic proteins with the Wnt signaling pathway

It is estimated that up to 20% of all types of human cancers worldwide are attributed to viruses. The genome of oncogenic viruses carries genes that have protein products that act as oncoproteins in cell proliferation and transformation. The modulation of cell cycle control mechanisms, cellular regulatory and signaling pathways by oncogenic viruses, plays an important role in viral carcinogenes...

Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin.

Membrane binding of the myristoylated alanine-rich C kinase substrate (MARCKS) requires both its myristate chain and basic "effector" region. Previous studies with a peptide corresponding to the effector region, MARCKS-(151-175), showed that the 13 basic residues interact electrostatically with acidic lipids and that the 5 hydrophobic phenylalanine residues penetrate the polar head group region...