1309975-48-1

Upstream product

• 2799-07-7 S-trityl-L-cysteine 
• 2937-50-0 Allyl chloroformate 
• 96865-72-4 (R)-2-allyloxycarbonylamino-3-tritylthio-propionic acid 
• 106-95-6 allyl bromide 

Relevant academic research and scientific papers

Design, synthesis, and anti-tumor activities of novel Brevinin-1BYa peptidomimetics

Brevinin-1BYa is an amphibian skin-derived peptide that exhibits promising anti-microbial activity against gram-positive and -negative bacteria. However, the anti-tumor activity of Brevinin-1BYa remains unclear, and, more importantly, its therapeutic application is limited owing to its poor protease and reduction stability. In this study, a series of novel Brevinin-1BYa derivatives, including O-linked N-acetyl-glucosamine glyclopeptides and disulfide bond mimetics, were designed and synthesized. Additionally, their anti-tumor activity against human prostate cancer cell line C4-2B, human NSCLC cell line A549 (adenocarcinoma), and human hepatoma cells line HuH-7 was investigated. Among these, the thioether bridge substituted peptidomimetic Brevinin-1BYa-3 displayed improved reduction stability, more stable secondary structure, greater protease stability, and increased anti-tumor activity compared with the original peptide, rendering it a promising leading compound for drug development, particularly for applications against malignant tumors.

Diaminodiacid bridge improves enzymatic and in vivo inhibitory activity of peptide CPI-1 against botulinum toxin serotype A

The replacement of the disulfide bridge of CPI-1, a peptide inhibitor of light chain of Botulinum toxin serotype A, with the thioether-containing and biscarba-containing diaminodiacid bridge leads to a significant decrease in the degradation by trypsin and increase in the detoxification activity in vivo, the addition of hydrophobic or positive amino acid at C-terminus of modified peptides further improves the inhibitory activity.

Diaminodiacid-based solid-phase synthesis of peptide disulfide bond mimics

The antimicrobial peptide tachyplesin I was used as a model to apply the title strategy, which was developed for the preparation of peptidic macrocycles with double disulfide surrogates. The folding and activity of the tachyplesin I analogues were found to be sensitive to the structure of the disulfide surrogates, thus underlining the necessity of a flexible synthetic route for generating disulfide bond surrogates with high structural diversity. Copyright

Synthesis and activity of thioether-containing analogues of the complement inhibitor compstatin

Disulfide bonds are essential for the structural stability and biological activity of many bioactive peptides. However, these bonds are labile to reducing agents, which can limit the therapeutic utility of such peptides. Substitution of a disulfide bond w