Abstract
As the risks posed by cancer and antibiotic-resistant bacteria to human health keep rising, extensive research has been dedicated to bioactive peptides. These peptides can trigger different physiological responses due to their remarkable specificity and affinity to cell surface receptors. The various biological and pharmaceutical functions of peptides present a wealth of opportunities, rendering them as promising candidates for therapeutic development. In this research, a novel peptide belonging to the Bowman-Birk type inhibitor (BBI) family, was isolated and identified from the skin secretion of the frog, Odorrana schmackeri. The biofunctionality was studied and several analogues were generated by rational structural modifications to the parent peptide for optimizing the antimicrobial or anticancer activities. Then, several strategies were used to modify a second type of trypsin inhibitor peptide to validate the rationale and effectiveness of the structural modification strategies. However, they all exerted a toxicity to normal cells (HaCaT). In conclusion, when TIL was conjugated with TAT, the biological functions were improved greatly especially on the antimicrobial activity, in addition, the residues linker (-GG-) seems to play an important promotion in the improvement of biological activities especially in the anticancer cell proliferation. Finally, the conjugation of cell penetrating peptides (CPPs) offers a compelling indication for exploring novel applications, suggesting potential avenues for peptide drug development.Thesis is embargoed until 31 July 2029.
| Date of Award | Jul 2024 |
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| Original language | English |
| Awarding Institution |
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| Supervisor | Mei Zhou (Supervisor) & Tianbao Chen (Supervisor) |