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oai:figshare.com:article/32641296 2026-10-01T16:24:22Z portal_1172 item_type_8 month_year_10_2026

Rational modification and bioactivity testing of antimicrobial peptides belonging to three different families from skin secretions of the frog, Rana pipiens Keyi Yao (23785062) PUREID: 641880177 Antimicrobial Peptides Rana pipiens Brevinin-1 Esculentin-2P Temporin-1P Antimicrobial peptides (AMPs) are key components of innate immunity and potential alternatives to antibiotics. Amphibian skin, particularly from frogs like Rana pipiens, is a rich source of diverse AMPs. This study reports the discovery and characterization of QUB-2578, a novel Brevinin-1 family AMP from R. pipiens, identified via molecular cloning. To explore intra-species AMP diversity, we also examined Esculentin-2P and Temporin-1P, previously reported in this species. Although their co-expression remains unconfirmed, these peptides provide a model for potential functional synergy. Through rational design, we generated analogues for each peptide: QUB-2578 variants via structure–activity relationship analysis, a truncated Esculentin-2P with non-natural substitutions, and a modified Temporin-1P with enhanced membrane activity. Functional assays revealed that several analogues showed improved antimicrobial efficacy, especially against Gram-negative bacteria, with reduced haemolysis and cytotoxicity. These findings support the idea that AMP structural diversity provides a multifaceted defense and that nature-inspired peptide engineering can yield improved antimicrobial candidates.<br><br><i>Thesis is embargoed until 31 July 2030.</i> 2026-10-01T16:24:22Z Text Thesis 10.17034/32641296.v1 https://figshare.com/articles/thesis/Rational_modification_and_bioactivity_testing_of_antimicrobial_peptides_belonging_to_three_different_families_from_skin_secretions_of_the_frog_Rana_pipiens/32641296 All Rights Reserved Open Access after 2029-07-31