Precision stabilization of α-helical peptide architectures—built to preserve conformation, improve binding, and enhance functional durability.
Helical peptides are conformationally controlled peptides engineered to adopt and maintain α-helical secondary structure under experimental or physiological conditions. Because many biologically critical interactions—especially protein–protein interactions (PPIs)—are mediated by α-helices, stabilizing a helix often improves potency, selectivity, and functional durability.
Unlike linear peptides that frequently lose helicity in solution, helix-stabilized peptides incorporate structural constraints (crosslinks, helix-promoting residues, or backbone modifications) that bias the peptide toward a defined conformation. We help select a stabilization strategy that fits your sequence, target interface, and downstream assay or delivery constraints.
Related constrained peptide services: Stapled Peptide Synthesis, Cyclic Peptide Synthesis, Macrocyclic Peptide Synthesis, Bicyclic Peptide Synthesis. For ready-made options, browse Catalog Peptides.
A helical peptide is defined by functionally relevant α-helix stabilization—not by a single synthetic method.
Helix stabilization is most useful when activity depends on presenting key side chains in a defined helical geometry.
Stapled peptides are a subset of helical peptides that use hydrocarbon crosslinks. Other chemistries can stabilize helices without hydrocarbon stapling.
If you provide these details, we can recommend a stabilization strategy and QC plan faster.
Side-chain crosslinking (commonly i,i+4 or i,i+7) to strongly enforce α-helicity; widely used for PPI targets.
Amide crosslinks between side chains to stabilize helix without hydrocarbon chemistry; useful for aqueous compatibility.
Cysteine-based constraints that can stabilize local structure; thioether options add redox stability vs disulfides.
α,α-disubstituted residues (e.g., Aib) and strategic substitutions to bias helix formation without crosslinks.
Backbone modification to tune conformation, permeability, and protease resistance (project-dependent feasibility).
Local constraints (including small rings or tethered motifs) to stabilize partial helices or turn/helix boundaries.
This distinction matters: helical peptides are a conformation-defined class, while stapled peptides are a chemistry-defined subset.
If you already know you need stapling, go directly to Stapled Peptide Synthesis. If you want the best helix strategy for your sequence, this helical peptide service is the right starting point.
Tell us what decision you need the data to support (screening, SAR, biophysics, or assay validation) and we’ll recommend a QC/characterization package that matches.
Use this as a practical checklist for quote requests. If you’re unsure, send your sequence(s) and goal—we’ll propose options.
No. Stapled peptides are one subset that use hydrocarbon crosslinks. Helical peptides may also be stabilized with lactam bridges, disulfide/thioether constraints, helix-promoting residues (e.g., Aib), or backbone modifications.
Choose helical peptides when activity depends on presenting residues in an α-helical geometry (common in PPIs). Cyclic/macrocyclic formats can constrain peptides too, but they do not automatically produce an α-helix unless designed for it.
Sequence(s), target or interface (if known), preferred helix span, required labels/handles, solubility/assay conditions, and your desired quantity/purity/QC. If you don’t know the strategy, send your goal and we’ll propose options.
Yes. Helical peptide programs commonly use analog series to tune helicity, affinity, and stability while keeping the binding epitope consistent.
We provide standard analytical QC (HPLC/MS). Optional CD spectroscopy can be added for helicity trend assessment when that data supports your decisions.
Yes. We can incorporate cysteine, azide/alkyne, linkers, and labels—planned to remain compatible with the selected helix stabilization chemistry.
Send your sequence and the interaction you’re targeting. We’ll recommend a stabilization path and a practical synthesis/QC plan aligned to your goals.
Also available: Catalog Peptides for ready-made, on-demand options.
Selected peer-reviewed literature on α-helix stabilization, stapled peptides, and conformational control in short sequences.
Trusted by biotech leaders worldwide for over 40+ years of delivering high quality, fast and scalable synthetic biology solutions.