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Data · dataset · 2026

The identification, modification and functional assessment of three novel bioactive peptides from the defensive skin secretion of Rana genus frogs

Listed in ZivaHub and Deakin Research Online and DMU Figshare — shown once because both records carry DOI 10.17034/32639496.v1

The overuse of traditional antibiotics has resulted in bacterial resistance and seriously compromised the therapeutic efficacy of the drugs, making the exploration of new antimicrobials particularly important.

Description

Several studies have shown that bio-active peptides have become an important source of new antimicrobial drugs due to their broad-spectrum antibacterial action and lack of susceptibility to resistance, and some of these peptides are already used in clinical therapy.

Antimicrobial peptides (AMPs) are available in a wide range of plants and animals, with amphibians being an important source. This study mainly focused on three bioactive peptides derived from different Rana genus frogs, and here were conducted a number of experiments to investigate their antibacterial activity and mechanisms, modified the peptide sequences to increase activity and decrease toxicity, and finally investigate the application of the peptides in various aspects based on their different activities.

Read the rest (2 more)

This research contained three experimental chapters. Based on the experimental results, the first peptide, QUB-1986, and the modified peptide, 2170-2R, were demonstrated to have increased antibacterial action when used in conjunction with antibiotics, as well as an inhibitory effect on various resistant P. aeruginosa strains in the first section. The second peptide, Hejiangin-B1, was modified in the second portion by the addition of hydrophobic amino acids to boost antibacterial action, indicating the effect of hydrophobicity on peptide activity, and by cyclisation to improve peptide stability in salt ion and enzyme environments.

The third portion primarily focused on the antimicrobial action of peptides in various acidic environments, with the study's fundamental rationale being to adjust the overall charge number of the peptide utilising the variation in pH.<br><br><i>Thesis is embargoed until 31 July 2029.</i>

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Provenance · 3 source records, 8 field assertions
SourceKeyLast seenRaw
ZivaHuboai:figshare.com:article/3263949613 d agoJSON v1
Deakin Research Onlineoai:figshare.com:article/3263949613 d agoJSON v1
DMU Figshareoai:figshare.com:article/3263949613 d agoJSON v1
FieldAssertionExtractorEvidence
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concepts[field].local:field:earth-environmentalmapping · figshare dmu ac ukconnector:figshare_dmu_ac_uk@1.0.0
concepts[field].local:field:earth-environmentalmapping · zivahub uct ac zaconnector:zivahub_uct_ac_za@1.0.0
concepts[field].local:field:earth-environmentalmapping · dro deakin edu auconnector:dro_deakin_edu_au@1.0.0
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titlesource · zivahub uct ac zaconnector:zivahub_uct_ac_za@1.0.0/metadata/dc/title