Site-defined, homogeneous sulfonated peptides (commonly referred to as sulfated peptides in biology) with defined modification site(s) and stoichiometry. Use sulfonated PTM peptides to map receptor binding, chemokine interactions, and create reliable assay controls.
Peptide sulfonation is often used as a practical service keyword for ordering modified peptides. In most biological literature, the dominant PTM is tyrosine sulfation (Tyr‑SO3H), a negatively charged modification that can dramatically change peptide–protein recognition—especially in extracellular signaling, chemokines, and GPCR ligand interactions.
Bio-Synthesis provides custom sulfonated peptide synthesis (peptide sulfonation / tyrosine sulfation, Tyr-SO₃H) as site-defined, homogeneous PTM peptides with controlled modification site(s) and stoichiometry. Our synthetic sulfonated (sulfated) peptides eliminate the heterogeneity typical of biological mixtures and are delivered with purification, LC–MS/HPLC QC, and COA for GPCR and chemokine binding, signaling studies, antibody validation, and assay-grade controls.
Related PTM services: PTM hub, acetylated peptides, methylated peptides, and phosphorylated peptides.
The most common biological form is tyrosine sulfation, typically written as Tyr(SO3H) or pTyr‑sulfate. We synthesize site-defined Tyr‑SO3H peptides for extracellular signaling and binding studies.
Sulfonation effects are often site- and state-dependent. Panels reduce false negatives and help identify the correct binding determinants.
If you’re unsure whether your target uses tyrosine sulfation, share the protein/ligand context and your assay—we’ll recommend the right format and controls.
Note: In biology, the standard term is tyrosine sulfation. Many customers search “sulfonated peptides,” so we use both terms for clarity.
SEO note: In biological contexts, these are often called sulfated peptides; many customers search for sulfated peptide synthesis as a synonym for sulfonated peptide synthesis.
Map sulfation-dependent recognition for GPCR ligands, chemokines, and extracellular signaling interactions.
Use site variants to locate the minimal sulfonation motif required for binding or activity.
Matched unmodified controls and sulfonated panels improve reproducibility and reduce ambiguous results.
If your target has multiple tyrosines, order a small site-variant panel—it’s the fastest way to identify the binding-critical sulfation site(s).
Tip: Share assay buffer, pH, and incubation time so we can recommend formats that preserve modification integrity and reduce redesign cycles.
Get sulfonated peptide synthesis with site-defined Tyr‑SO3H, matched controls, and assay-ready QC (LC–MS/HPLC + COA).
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Many extracellular interactions change dramatically with Tyr‑SO3H. Talk with a peptide chemist to choose the right sites, controls, and panel design.
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In most biological contexts, the canonical PTM is tyrosine sulfation (Tyr‑SO3H). Many customers search “sulfonated peptides,” so we use both terms and clarify the specific modification being synthesized.
Yes. Research-grade sulfonated/sulfated peptides are typically chemically synthesized so the modification is installed at defined residue positions and stoichiometry. This avoids heterogeneity and supports reproducible binding and functional assays.
Yes. For most studies, we recommend an unmodified matched control plus site variants when multiple tyrosines are present. This isolates the sulfation-dependent contribution to binding or activity.
Often, yes. If you need additional PTMs or workflow handles (e.g., biotin or fluorescence), share your design and we’ll recommend a format that preserves the key sulfation state.
Background on tyrosine sulfation, extracellular signaling, and binding specificity.
Want a tailored reading list for your receptor/chemokine target? Share your system and we’ll recommend key references and panel designs.
Share sequence, sulfonation/sulfation site(s), desired pattern (single vs multi), purity, quantity, and application.
Need help choosing sites or controls? We’ll recommend an efficient panel design for sulfation-dependent binding or signaling assays.
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