Magainin 2
From Proteopedia
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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 bind to the bacterial membrane and perform it's antimicrobial action. | + | 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. |
==Crystalization of Ala-Magainin== | ==Crystalization of Ala-Magainin== | ||
So far we had shown Magainin 2 structure based only on NMR findings, Because helical AMPs crystallography is limited, since it is hard to form crystals. | So far we had shown Magainin 2 structure based only on NMR findings, Because helical AMPs crystallography is limited, since it is hard to form crystals. | ||
| - | In the | + | In the Hayouka et al., 2013, In order to perform crystallization of Magainin 2, changes in the sequence were maid, and Ala-Magainin 2 was contsructed. In Ala-magainin one Ser (S) and two Gly (G) residues have been changed to Ala (A) in order to increase helical propensity. These changes were resulted only in minor changes in the secondary syructure (ala-magainin has a few more residues in alpha helix structure). |
Revision as of 10:06, 23 January 2015
Magainin 2
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
