Magainin 2: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 20: | Line 20: | ||
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: | 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: | ||
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. | 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, and the other side contains all cationic residues. this probably helps Magainin 2 to | 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, and the other side contains all cationic residues. this probably helps Magainin 2 to bind to the bacterial membrane and perform it's antimicrobial action. | ||
==Crystalization of Ala-Magainin== | |||
So far we had shown Magainin 2 structure based only on NMR findings, since it is very hard to perform crystalization of peptides. | |||