Antimicrobial peptides: Difference between revisions
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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 porcine leukocytes 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 porcine leukocytes 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>. | ||
=Secondary structure= | ===Secondary structure=== | ||
AMPs structure allows them to interact with negatively charged phospholipid head groups of microbial membranes, resulting in pore formation (or other mechanism, ) on the bacterial membrane . | AMPs structure allows them to interact with negatively charged phospholipid head groups of microbial membranes, resulting in pore formation (or other mechanism, ) on the bacterial membrane . | ||
