Antimicrobial peptides

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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>.
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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. Their structure allow them to interact with negatively charged phospholipid head groups of microbial membranes, resulting in pore formation on the bacterial membrane .�
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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.
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Nevertheless, the way different antimicrobial peptides achieve their goal appears to be different.
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===Suggested Mechanisms===
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Their structure allow them to interact with negatively charged phospholipid head groups of microbial membranes, resulting in pore formation on the bacterial membrane .
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Nevertheless, the way different antimicrobial peptides achieve their goal appears to be different, and there are a few suggested mechanisms.
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===Suggested Mechanisms===
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there are a few suggested machanisms of how AMPs work(William C. Wimley,
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ACS CHEMICAL BIOLOGY, 2010). they can be divided into two:
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(A) Transmembrane Pore Models of AMP Membrane Activity and (B) Nonpore Models of AMP Activity
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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.
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== Function ==
== Function ==

Revision as of 08:08, 12 January 2015

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PDB ID 3rec

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References

  1. 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
  2. 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

Proteopedia Page Contributors and Editors (what is this?)

Tal stern, Carmit Ginesin, Michal Harel

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