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Research

We are working on:
Synthetic biology
Antimicrobial peptides
Biomolecular interactions.

Recent Research Highlights

: research

How do antimicrobial peptides work? Dr. Allison Langham and Professor Yiannis Kaznessis, Department of Chemical Engineering and Materials Science, simulated the pore that is formed by protegrin-1, a potent antimicrobial peptide, in the lipid bilayer membrane of bacteria. The simulations show exactly how a protegrin pore allows ions and other cell contents to leak out of the bacterion, causing its death. In the picture, the cross sectional view of a protegrin-1 pore (in green) in a lipid bilayer is shown (lipid chains in grey and lipid heads in red; water is cyan). The movement of ions through the pore was visualized using molecular dynamics simulations (in yellow, a chloride ion is shown as it moves through the pore). This information helps to elucidate the mechanism of action by which this antimicrobial peptide kills bacteria and rationalizes engineering of novel, potent antibiotic molecules. The top view of the full system is shown in the insert.

 

 

 
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