Data · dataset · 2026
Studies on the discovery and bioactivity of a Kunitz peptide: antimicrobial activity assessment and generic fragments for improved antimicrobial activity
Listed in ZivaHub and Deakin Research Online and DMU Figshare — shown once because both records carry DOI 10.17034/32639490.v1
Antimicrobial peptides have been considered good candidates for development as new antimicrobial reagents due to their rapid action, broad-spectrum antibacterial activity and low cytotoxicity.
Description
QUB-1939 is a novel peptide derived from Odorrana livida, which has been discovered to have some interesting bioactivities, including antimicrobial and trypsin inhibition functions. Focusing on its antibacterial activity and analogue design, the internal motif -KVKF-, was repeated several times to produce a series of peptides, which demonstrated much better antimicrobial functions.
A mechanistic study found that QUB-1939 and its analogues possessed membrane permeabilising effects Gram-negative bacteria and demonstrated bactericidal activity on MRSA, by entering cells through the cell membrane to influence internal physiological processes. QUB-1939 and its analogues have environmental stability at different temperatures, salt ion concentrations, and serum concentrations and display a trypsin stability characteristic.
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The toxicity assessments include a haemolysis effect study, an antiproliferative study on normal human and rat cells, and a therapeutic index study. Combining these assessments, QUB-2442 and QUB-3060 were the safest peptides with potential to be developed as antimicrobial reagents. A further study also demonstrated that these two peptides also displayed potent antimicrobial activity on drug-resistant E. coli and K. pneumoniae.
LPS and LTA were the two targets of QUB-2442 and QUB-3060. The whole blood environment also had little influence on the antimicrobial activity of these peptides. After making research on the motif itself, QUB-1023 and QUB-1525 had great antimicrobial activity.
However, QUB-1525 repeated the motif two times had high toxicity to HaCat and blood cells. With the purpose to identify whether the motif can provide a new antimicrobial improvement strategy, the motif added in Temporin-A. TA series peptides prove that motif can improve different AMPs antimicrobial activity.<br><i><br>Thesis embargoed until 31 July 2029.</i>
Links
Where it is published
- DOI doi.org/10.17034/32639490.v1 ↗
DOI / persistent id · from zivahub uct ac za
Catalogue records · 1
- OAI-PMH record api.figshare.com/v2/oai?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Af… ↗
metadata API · from zivahub uct ac za
Topics
Provenance · 3 source records, 8 field assertions
| Source | Key | Last seen | Raw |
|---|---|---|---|
| ZivaHub | oai:figshare.com:article/32639490 | 10 d ago | JSON v1 |
| Deakin Research Online | oai:figshare.com:article/32639490 | 10 d ago | JSON v1 |
| DMU Figshare | oai:figshare.com:article/32639490 | 10 d ago | JSON v1 |
| Field | Assertion | Extractor | Evidence |
|---|---|---|---|
| access_level | source · zivahub uct ac za | connector:zivahub_uct_ac_za@1.0.0 | |
| concepts[field].local:field:earth-environmental | mapping · figshare dmu ac uk | connector:figshare_dmu_ac_uk@1.0.0 | |
| concepts[field].local:field:earth-environmental | mapping · zivahub uct ac za | connector:zivahub_uct_ac_za@1.0.0 | |
| concepts[field].local:field:earth-environmental | mapping · dro deakin edu au | connector:dro_deakin_edu_au@1.0.0 | |
| description | source · zivahub uct ac za | connector:zivahub_uct_ac_za@1.0.0 | /metadata/dc/description |
| license_text | source · zivahub uct ac za | connector:zivahub_uct_ac_za@1.0.0 | |
| publication_date | source · zivahub uct ac za | connector:zivahub_uct_ac_za@1.0.0 | |
| title | source · zivahub uct ac za | connector:zivahub_uct_ac_za@1.0.0 | /metadata/dc/title |