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The Joseph A. Dixon Travel Award 2001 Spring ACS Meeting, San Diego, CA
Lysine
7: Key residue for melittin cytolytic activity Preliminary molecular modeling results (semi-empirical) from our lab suggest that melittin may form a pore in a membrane due to electrostatic repulsion initially generated by the cooperation of two amino acid residues: the first is a proline that forms a kink at the position 14 in melittin and the second is a charged lysine residue at position 7. Also, molecular dynamic calculations predict that melittin forms an aggregate of four antiparallel molecules whose charged lysine residues are situated in the middle of the melittin hydrophobic helices which are located near the membrane leaflet junction. The orientation of these peptides depends on the charged “melittin tail” and may lead to a squashing of the membrane. Further modeling is needed to determine the mechanism of the lysine-7 and proline-14 in attracting negatively charged ions that invade the membrane causing a complete cell lysis. The Nittany Chemistry Trail No abstract available |
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