Antimicrobial peptides: Difference between revisions
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'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel. | '''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel. | ||
[[Image:Barrel stave pore model.JPG|right| | [[Image:Barrel stave pore model.JPG|right|350px]] | ||
'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure.. | '''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure.. | ||
[[Image:Torodial pore model.JPG]] | [[Image:Torodial pore model.JPG|right|350px]] | ||
the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms: | the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms: | ||
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'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration. | '''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration. | ||
[[Image:Detergent model.JPG]] | [[Image:Detergent model.JPG|right|350px]] | ||
