Antimicrobial peptides: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 19: | Line 19: | ||
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. 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. | |||
===Suggested Mechanisms=== | |||
== Function == | == Function == | ||
Revision as of 07:59, 12 January 2015
Your Heading Here (maybe something like 'Structure')
| |||||||||||