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]] | [[Image:Barrel stave pore model.JPG]] | ||
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: | [[Image:Torodial pore model.JPG]] | ||
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: | ||
1- The carpet model. In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization. | 1- The carpet model. In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization. | ||
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: | [[Image:Detergent model.JPG]] | ||