Antimicrobial peptides
From Proteopedia
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AMPs are rich with hydrophibic (Ala, Val, Ile, Leu, Met, Phe, Tyr, Trp) and Possitively charged (Lys, Arg) Amino Acids, which seems to allow them to bind into membranes. <scene name='67/676980/1pg1_arginine/1'>Protegrin 1</scene>, is a peptide from........... and it's sequence is rich with <scene name='67/676980/1pg1_hydrophobic_residues/1'> hydrophobic residues</scene> and <scene name='67/676980/1pg1_cationic_residues/1'>cationic residues</scene>. | AMPs are rich with hydrophibic (Ala, Val, Ile, Leu, Met, Phe, Tyr, Trp) and Possitively charged (Lys, Arg) Amino Acids, which seems to allow them to bind into membranes. <scene name='67/676980/1pg1_arginine/1'>Protegrin 1</scene>, is a peptide from........... and it's sequence is rich with <scene name='67/676980/1pg1_hydrophobic_residues/1'> hydrophobic residues</scene> and <scene name='67/676980/1pg1_cationic_residues/1'>cationic residues</scene>. | ||
- | AMPs have a big vareity of structures, and these structures can be divided to a few categories: alpha helix structures, beta sheet structures, and peptides with extended or loop structures | + | AMPs have a big vareity of structures, and these structures can be divided to a few categories: alpha helix structures, beta sheet structures, and peptides with extended or loop structures. |
- | + | ||
- | ===Suggested Mechanisms=== | + | Their structure allow them to interact with negatively charged phospholipid head groups of microbial membranes, resulting in pore formation on the bacterial membrane . |
+ | Nevertheless, the way different antimicrobial peptides achieve their goal appears to be different, and there are a few suggested mechanisms. | ||
+ | |||
+ | ===Suggested Mechanisms=== | ||
+ | there are a few suggested machanisms of how AMPs work(William C. Wimley, | ||
+ | ACS CHEMICAL BIOLOGY, 2010). they can be divided into two: | ||
+ | (A) Transmembrane Pore Models of AMP Membrane Activity and (B) Nonpore Models of AMP Activity | ||
+ | |||
+ | In the Transmembrane Pore Models, it is suggested that AMPs form many pores in the mambrane, so that iit cannot hole it's content anymore. | ||
+ | |||
== Function == | == Function == | ||
Revision as of 08:08, 12 January 2015
Your Heading Here (maybe something like 'Structure')
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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