Identification, modification and functional evaluation of antimicrobial peptides from the skin secretions of Anuran species

While hydrophobicity reduction effectively lowered toxicity in Brevinin-1-LFc, this strategy proved less effective for QUB-2579, suggesting that structural differences and amino acid substitutions influence their functional outcomes. In contrast, QUB-2155 demonstrated strong antimicrobial activity with low haemolysis, making it a promising drug candidate. Increasing its hydrophobicity enhanced antimicrobial efficacy but also raised toxicity, underscoring the challenge of balancing these properties.<br><br>All peptides were found to adopt α-helical structures and exert their effects through membrane disruption, an advantage over conventional antibiotics due to the lower likelihood of resistance development.

This study highlights the importance of structural and physicochemical optimization in AMP design. Future work should focus on alternative modification strategies, novel delivery systems, and in vivo validation to advance these peptides toward clinical applications. With further refinement, AMPs have the potential to become next-generation antimicrobial agents in the fight against multidrug-resistant pathogens.<br><br><i>Thesis embargoed until 31st July 2030.</i><br>