Design, synthesis, and biological evaluation of stapled ascaphin-8 peptides.
Ascaphin-8 is an α-helical anti-tumor and antimicrobial peptide containing 19 residues, which was isolated from norepinephrine-stimulated skin secretions of the North American tailed frog Ascaphus truei. To improve both its stability and biological activities, a series of hydrocarbon-stapled analogs of Ascaphin-8 were synthesized and investigated for their potential antiproliferative activities. The activity studies were evaluated using the CCK-8 method and colony formation assay on human cancer cell lines. Ascaphin-8-3, as the most active peptide, showed a stronger inhibition effect when compared with the parent peptide for the tested cell lines. In addition, the effect of Ascaphin-8-3 on inhibiting the metastatic capabilities of A549 cells was more powerful than that of the parent peptide. This peptide derivative showed potentiality for further optimization in antitumor drugs.
['Liu|Jing|J|', 'Chen|Si|S|', 'Chai|Xiao-Yun|XY|', 'Gao|Fei|F|', 'Wang|Chen|C|', 'Tang|Hua|H|', 'Li|Xiang|X|', 'Liu|Ying|Y|', 'Hu|Hong-Gang|HG|']
D023181:Antimicrobial Cationic Peptides D002465:Cell Movement D002470:Cell Survival D002478:Cells, Cultured D004305:Dose-Response Relationship, Drug D015195:Drug Design D006801:Humans D015394:Molecular Structure D013329:Structure-Activity Relationship
Ascaphin-8 Anti-tumor AMP Stapled peptide