Studies on the structure-function relationships of novel peptides isolated from <i>Odorrana grahami</i>

The parent peptide has a broad-spectrum antimicrobial activity against all the pathogens tested herein. Analogues of it exhibited advantages and disadvantages in many ways, mainly in their antimicrobial activity effects. This study has revealed the rationality of the imperfect amphipathic model and possibility of further modification targeting the residues of the hydrophobic face.

Additionally, the disulfide bond also has been shown to have a special influence on anti-biofilm activity. Further structure-function relationship studies could be performed based on the bio-functionality data of these analogues presented here. <br><br>In Chapter 5, another peptide isolated from the same frog above, which was studied before and showed no antimicrobial activity, was revisited. This peptide, possessing lectin-like activity and specific immune system bio-functions, underwent structural modifications in an attempt to investigate structure-function relationships for analogue design as potential drug leads.

However, these attempts proved unsuccessful. <br><br>Key word: Drug-resistance, Antimicrobial peptides, Amphibians, Brevinin-1 peptide family, Anti-biofilm peptides<br><br><i>Thesis is embargoed until 31 July 2028</i>.<br><br>