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Title: Binding and bending : the interaction of magainin-II with lipid bilayers
Author: Dodd, Alan John
ISNI:       0000 0004 2671 7368
Current Institution: University of Bristol
Date of Award: 2008
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An understanding of the action of the helical antimicrobial peptide magainin II has significance clinically, since the peptide has broad spectrum antimicrobial, tumouricidal and antifungal activity through its ability to create pores in membranes. To better understand the mechanism of action of this peptide, a joint approach of simulations and experiment was used to determine the factors involved in pore formation by magainin II. Previous studies involving a cysteine-crosslinked mutant indicated that dimerisation of magainin II may be a key step in the insertion mechanism, and atomic detail molecular dynamics simulations have supported the theory that this is due to an inability of the membrane to accommodate the larger bulk of a parallel dimer without significant distortion.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available