RAWSON, Kirstie Marie (2019). Antimicrobial Peptides from Venom: Structure, Function and Toxicity. Doctoral, Sheffield Hallam University.
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Rawson_2019_PhD_AntimicrobialPeptidesVenom.pdf - Accepted Version
Available under License Creative Commons Attribution Non-commercial No Derivatives.
Rawson_2019_PhD_AntimicrobialPeptidesVenom.pdf - Accepted Version
Available under License Creative Commons Attribution Non-commercial No Derivatives.
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Abstract
The need for new antimicrobials with novel mechanisms of action is becoming
one of the most urgent requirements in modern medicine. Antimicrobial peptides
(AMPs) are naturally occurring compounds which possess a rapid killing
mechanism and low resistance potential. Consequently, they are being viewed
as potential alternatives to traditional antibiotics. One of the major factors limiting
further development of AMPs is off target toxicity. Enhancements to antimicrobial
peptides which can maximise antimicrobial activity whilst reducing mammalian
cytotoxicity would make these peptides more attractive as future
pharmaceuticals.
Smp24 and Smp43 are AMPs derived from the venom of the scorpion Scorpio
maurus palmatus. This study sought to better understand the relationship
between structure, function and bacterial selectivity of these peptides by
performing single amino acid substitutions. The structure-function relationship of
the two AMPs has been investigated by performing N-terminal, mid-chain and Cterminal
amino acid substitutions and determining the effect this has on the
antimicrobial and cytotoxic activity of the peptides. The structural implications of
the amino acid substitutions have been investigated via homology modelling and
circular dichroism spectroscopy.
Functional improvements have been made to modified peptides when compared
with native Smp24 and native Smp43, which have produced peptides with
enhanced therapeutic indices.
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