Stapled Peptide Synthesis

" What Are Stapled Peptides? "

Stapled peptides were developed based on the need for peptides to form an α-helix to enter the cell through the cell membrane. It has been shown that peptides with α-helical structures and enriched with positive charges can cross cell membranes. Therefore, α-helical structures using disulfide bonds and intramolecular amide bonds as scaffolds have been developed, but none of these scaffolds can be stabilized in physiological environments. In 2000, Verdine et al. developed a method of stabilizing the α-helical structure of peptides by using carbon-carbon bonds as scaffolds, and peptides obtained by this method called stapled peptides. Stapled peptides have the advantages of higher degree of α-helix, strong binding ability, ability to pass through the cell membrane, difficult to be hydrolyzed by protease, and long half-life in the organism.

What We Offer

The application of stapled peptides in drug discovery and development has gained significant attention due to their ability to modulate protein-protein interactions. Several research studies have demonstrated the potential of stapled peptides as novel therapeutics for various diseases, including cancer, viral infections, and autoimmune disorders. As a biotechnology company specializing in peptide synthesis, Alfa Chemistry offer comprehensive stapled peptide synthesis services to meet the various requirements of researchers and pharmaceutical companies. In addition, our expertise in custom peptide synthesis allows us to design and synthesize stapled peptides with high purity, precision, and quality, ensuring the successful integration of stapled peptides into drug discovery programs. Whether you require stapled peptides for basic research, preclinical studies, or therapeutic development, our services can support you in exploring the therapeutic potential of stapled peptides in a variety of biomedical applications.

Synthetic Strategy

Stapled peptides are typically prepared using Fmoc-solid phase peptide synthesis. Specifically, two non-natural amino acids containing α-methyl, α-alkenyl groups are introduced during the solid-phase synthesis of peptide chains, and then an ring-closing olefin metathesis (RCM) reaction occurs between the two non-natural amino acids, which constitutes an all-carbon scaffold that stabilizes the α-helical structural conformation, and thus synthesizes the stapled peptide.

Our Advantages

Strict quality system
Alfa Chemistry has a comprehensive quality control management platform. We can provide you with chromatograms and mass spectrum reports, and can also provide special services according to your needs.

Stable product quality
Alfa Chemistry has a fully automated production platform to ensure the batch-to-batch stability of stapled peptides and always provide high-quality stapled peptide products, from mg level to kilogram level.

Guaranteeing sufficient delivery
Alfa Chemistry ensure that each stapled peptide synthesized is delivered in sufficient quantity to avoid the risk of insufficient quantity.

Efficient service
Alfa Chemistry provide one-on-one project services and communicate with you regularly about project progress through meetings.

Fast delivery cycle
Delivery takes 2-3 weeks, shortening your waiting time.

Reasonable price system
Alfa Chemistry provide the most competitive prices based on your product requirements and order quantity.

Strict confidentiality
Once cooperation is reached, Alfa Chemistry will sign a confidentiality agreement with you.

Service Process