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Studying the interaction between cardiolipin-based supported lipid membranes and amphiphilic antimicrobial peptides

Terrmin

HT23

Beskrivning

Cationic amphiphilic peptides have attracted considerable interest in novel pharmaceutical applications as they hold potential as a new class of antibiotics and anticancer agents. There, are, however, many challenges concerning the administration of these peptides. Peptides in free form are subject to rapid enzymatic degradation and fast renal filtrations. Formulating peptides in suitable nanoparticles, can help prevent both these effects. It has been shown, e.g., that melittin (a peptide isolated from honey bee venom) is protected against these detrimental effects if it is formulated into lipodisks (open lipid-bilayer nanostructures).
Cardiolipin is a natural occurring lipid found mainly in mitochondria membranes. The lipid is different from other phospholipids as it contains four fatty acid chains instead of only two. It has been hypothesized that cardiolipin-based lipid bilayer structures should be able also to incorporate large amounts of melittin without compromising their structural integrity.
In this project you will characterize the binding of melittin to cardiolipin-based supported lipid membrane structures. The studies will be based in surface sensitive techniques such as the quartz crystal microbalance with dissipation monitoring. The results will allow evaluating whether cardiolipin-based lipid membrane structures can be suitable delivery vehicles for cationic amphiphilic peptides.

Huvudområde

Farmaceutisk kemi

Ämne

Fysikalisk kemi

Typ

Laborativ studie

Företag

Uppsala Universitet

Ort/Plats

Uppsala

Handledarens namn

Victor Agmo Hernandez

Handledarens e-post

victor.agmo@ilk.uu.se

Institution

Institutionen för Läkemedelskemi

Program

Receptarieprogrammet

Kurs

Fördjupningsprojekt i Farmaceutisk fysikalisk kemi, 15.0 hp - 3FC410

Omfattning/hp

15hp