Year: 2024
Type: conference-abstract
Abstract: Aurein 1.2 was chosen as a template for rational modification to achieve a higher biofunctionality.The modifications of the six new analogues were made in the primary structure by incorporating unnatural amino acids in order to improve the pharmacodynamics of the new peptides.Aurein 1.2 was modified at position 7 and 8.The six new modified analogs followed the structure:where Xxx is Orn or Dab (diaminobutyric acid).Lysine residues were replaced sequentially and simultaneously with the unnatural amino acids. CONCLUSIONSAntimicrobial peptides are identified as the most promising option to the conventional molecules used nowadays against infections because they mimic the natural metabolic effects within the body with low toxicity and better selectivity which proves they're one of the alternatives for therapeutic intervention.Aurein 1.2 is a short multi-functional antimicrobial peptide isolated from Litoria aurea and Litoria raniformis skin secretion.Aurein peptides can be classified into five distinct groups (Aureins -1 to -5), among which Aurein-1 peptides are considered to be one of the shortest α-helical peptides with antimicrobial and anticancer activity.Many antimicrobial peptides have the ability to cross cell membranes and destroy bacteria.Biological activity of Aurein has been widely investigated however, its lack of a potent action failed to provide Aurein 1.2 with a competitive edge for further development as a therapeutic agent for clinical use.
Source: European Peptide Symposium (EPS)
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: bronze
Funder: European Commission
Award: G7575274431
OpenAlex ID: W4403085975