Stabilize bioactive conformations
Cyclic, stapled, macrocyclic, bicyclic, and helical peptide formats engineered for stability, specificity, and performance.
Looking for a hub? Return to Advanced Peptide Synthesis.
Bio-Synthesis provides constrained and conformationally controlled peptide synthesis services including cyclic peptide synthesis, stapled peptide synthesis, macrocyclic peptide synthesis, bicyclic peptide synthesis, and helical/constrained peptide design. These formats reduce conformational flexibility to stabilize bioactive structure, improve apparent affinity, and increase protease resistance—often translating to better reproducibility in binding assays and improved functional performance.
Best-fit when you need
Reduce conformer heterogeneity for consistent binding.
Increase protease resistance and shelf stability.
Stabilize the bioactive geometry for higher potency.
Use this table to map your project to the right constraint strategy. For detailed options, see the service sections below.
Related service pages (internal links)
For full options and examples, visit the dedicated service pages:
Cyclic peptide synthesis introduces ring closure to reduce flexibility and stabilize binding geometry. Cycles can be formed head-to-tail or via side-chain linkages depending on sequence and desired topology.
Related: Cyclic peptide synthesis service page.
Stapled peptide synthesis stabilizes alpha-helical structure via a side-chain staple, often improving protease resistance and target engagement for helix-mediated interactions.
Related: Stapled peptide synthesis service page.
Macrocyclic peptide synthesis creates larger ring systems that can improve stability and selectivity by constraining peptides into productive conformations while maintaining surface area for binding.
Related: Macrocyclic peptide synthesis service page.
Bicyclic peptide synthesis creates two interconnected rings for higher rigidity and controlled presentation. This can improve specificity and affinity for challenging targets where single constraints are insufficient.
Related: Bicyclic peptide synthesis service page.
Helical/constrained peptides bias secondary structure (often alpha helices) using helix-promoting residues, short constraints, or design features that stabilize the bioactive presentation.
Related: Helical / constrained peptides service page.
Cyclic peptides reduce flexibility by ring closure and are broadly useful for stability and binding geometry control. Stapled peptides specifically stabilize helical structure and are often used for helix-mediated targets (e.g., PPIs).
Macrocyclic peptides have one ring; bicyclic peptides have two rings. Bicycles are typically more rigid and can improve specificity and affinity for difficult targets.
In addition to standard LC–MS and purity, some projects benefit from extra confirmation of cyclization/stapling success, disulfide state, or mapping to ensure reproducibility.
Yes. Common add-ons include cysteine, click handles, biotin, dyes, and cleavable linkers—when planned into the design.
Sequence(s), proposed linkage sites, desired ring size/strategy, target purity/scale, and any required handles. If you have a target or assay, include it to inform constraint selection.
If your bioactive conformation is helical, helical/constrained designs (including stapling) are often best. If broader conformational restriction is needed, macrocycles can provide strong stabilization while preserving binding surface area.
Share your sequence(s), target conformation (cyclic/stapled/macrocyclic/bicyclic/helical), any required linkers/handles, and the intended application. We’ll recommend practical specifications and a synthesis/QC plan aligned to your goals.
Tip: If the peptide is hydrophobic/long/cysteine-rich, include that context so we can route the request to the right synthesis strategy.
Trusted by biotech leaders worldwide for over 40+ years of delivering high quality, fast and scalable synthetic biology solutions.