Magainin 2: Difference between revisions

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== Structural highlights ==

In general, amphipathic helical peptides that disrupt the ionic gradient of cells are thought to do so by forming ion channels assembled from 4–6 peptide molecules. ��It was thought that this mechanism is also acountable for Magainin 2, But earlier solid-state NMR results show that its helix axis lies in the plane of phospholipid bilayers, suggesting that magainin’s mechanism for disrupting the ionic gradient may be fundamentally different.

~~The mechanism of how magainin 2 works is~~ approximated to be the pore model, of which each single unit bind to the membrane and form a small pore, and when a few units bind to the membrane this way, the insides of the cell leak outside and the cell dies. Magainin 2 structure allows it to do so:

approximated to be the pore model, of which each single unit bind to the membrane and form a small pore, and when a few units bind to the membrane this way, the insides of the cell leak outside and the cell dies. Magainin 2 structure allows it to do so:

Magainin 2, As typical to all AMPs, Is rich with <scene name='69/692248/Mag2_cationic_residues/2'>cationic residues</scene> that allow it to interact with Bacterial membranes, that are negatively charged in phosiological pH, and rich with <scene name='69/692248/Mag2_hydrophobic_residues/1'>Hydrophobic residues</scene> that allow it to interact with the membrane's phospholipids.

We can see <scene name='69/692248/Mag2_hydrophobic_and_cationic/1'>here</scene> that the residues are organised in it's alpha helix in a way that one side contains all hydrophobic residues (shown in green), and the other side contains all cationic residues (shown in purple). this probably helps Magainin 2 to bind to the bacterial membrane and perform it's antimicrobial action.

Magainin 2: Difference between revisions

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@@ Line 16: / Line 16: @@
 == Structural highlights ==
+In general, amphipathic helical peptides that disrupt the ionic gradient of cells are thought to do so by forming ion channels assembled from 4–6 peptide molecules. ��It was thought that this mechanism is also acountable for Magainin 2, But earlier solid-state NMR results show that its helix axis lies in the plane of phospholipid bilayers, suggesting that magainin’s mechanism for disrupting the ionic gradient may be fundamentally different.
-The mechanism of how magainin 2 works is approximated to be the pore model, of which each single unit bind to the membrane and form a small pore, and when a few units bind to the membrane this way, the insides of the cell leak outside and the cell dies. Magainin 2 structure allows it to do so:
+approximated to be the pore model, of which each single unit bind to the membrane and form a small pore, and when a few units bind to the membrane this way, the insides of the cell leak outside and the cell dies. Magainin 2 structure allows it to do so:
 Magainin 2, As typical to all AMPs, Is rich with <scene name='69/692248/Mag2_cationic_residues/2'>cationic residues</scene> that allow it to interact with Bacterial membranes, that are negatively charged in phosiological pH, and rich with <scene name='69/692248/Mag2_hydrophobic_residues/1'>Hydrophobic residues</scene> that allow it to interact with the membrane's phospholipids.
 We can see <scene name='69/692248/Mag2_hydrophobic_and_cationic/1'>here</scene> that the residues are organised in it's alpha helix in a way that one side contains all hydrophobic residues (shown in green), and the other side contains all cationic residues (shown in purple). this probably helps Magainin 2 to bind to the bacterial membrane and perform it's antimicrobial action.